Kay Oliver Schink

• Kostas, Michal Janusz; Munthe, Else; Haugsten, Ellen Margrethe; Mateus, Duarte Nunes de Carvalho; Sørensen, Vigdis & Lærdahl, Jon Kristen [Show all 13 contributors for this article] (2026). Unconventional activation of the proto-oncogene FGFR1 by extracellular phosphate via H<inf>2</inf>O<inf>2</inf>-mediated kinase oxidation. Cell reports. 45(6). doi: 10.1016/j.celrep.2026.117504. Full text in Research Archive
• Freitag, Johannes; Schink, Kay Oliver & Bange, Gert (2025). Innere und äußere Selbstorganisation von Peroxisomen. BioSpektrum. ISSN 0947-0867. 31(6), p. 639–641. doi: 10.1007/s12268-025-2561-2. Full text in Research Archive Show summary

  Peroxisomes are eukaryotic organelles for fatty acid oxidation and other metabolic tasks. They can differentiate into subpopulations via lumenal cores leading to uneven enzyme distribution and metabolic comaprtmentalization. Externally, they interact with other organelles at contact sites, supporting dynamic cellular positioning and metabolic cooperation.

• Medhus, Astrid; Schink, Kay Oliver; Longva, Ane Sager; Engebråten, Olav; Berg, Kristian & Weyergang, Anette (2025). The mechanisms of HER2 targeted ADCs are dependent on Rab GTPases. Therapeutic Advances in Medical Oncology. ISSN 1758-8340. 17. doi: 10.1177/17588359251332473. Full text in Research Archive Show summary

  Introduction: In the era of personalized cancer therapy, antibody-drug conjugates (ADCs) have become one of the fastest-emerging groups of anticancer drugs. ADCs consist of an antibody coupled to a cytotoxic payload by a chemical linker, designed to be cleaved off intracellularly. Understanding the intracellular trafficking and processing of ADCs is crucial for elucidating their mechanism of action. Objective: This study aimed to compare trastuzumab deruxtecan (T-DXd) to ado-trastuzumab emtansine (T-DM1) with emphasis on Rab GTPase-regulated intracellular trafficking and its impact on ADC efficacy. Methods: The efficacy of T-DXd and T-DM1 was assessed in a panel of HER2-positive cell lines. Correlations between ADC efficacy and the expression of HER2 and Rab GTPases were evaluated. Functional studies, including knockdown (KD), overexpression, and microscopy, were performed to evaluate the impact of Rab GTPases on ADC cytotoxicity. Results: In contrast to T-DM1, T-DXd efficacy was found not to correlate to HER2 expression in a panel of HER2-positive cell lines. However, a correlation to RAB5A expression was found for T-DXd efficacy, although not as strong as for T-DM1. Altering the expression of RAB5 in our model system confirmed RAB5 to have an impact on both T-DXd and T-DM1 cytotoxicity, but more on T-DM1. In addition, RAB4a was found to influence T-DXd sensitivity, but not T-DM1, indicating differences in intracellular processing between T-DXd and T-DM1. Conclusion: The study demonstrates that ADC design significantly influences intracellular trafficking and processing. The linker design, in particular, plays a major role in determining the intracellular fate of an ADC.

• Bäcker, Nils; Ast, Julia; Martorana, Domenica; Renicke, Christian; Berger, Jil & Mais, Cristopher-Nils [Show all 18 contributors for this article] (2025). Peroxisomal core structures segregate diverse metabolic pathways. Nature Communications. 16. doi: 10.1038/s41467-025-57053-9. Full text in Research Archive Show summary

  Peroxisomes are single membrane-bounded oxidative organelles with various metabolic functions including β-oxidation of fatty acids. Peroxisomes of many species confine certain metabolic enzymes into sub-compartments sometimes visible as electron dense cores. Why these structures form is largely unknown. Here, we report that in the smut fungus Ustilago maydis detergent resistant core structures are enriched for different enzymes excluding several key enzymes of the β-oxidation pathway. This confinement contributes to generation of peroxisome subpopulations that differ in their enzyme content. We identify short amino acid motifs necessary and sufficient for protein self-assembly into aggregates in vitro. The motifs trigger enrichment in cores in vivo and are active in mammalian cells. Perturbation of core assembly via variation of such motifs affects peroxisome function in U. maydis strains challenged with fatty acids. Thus, protein core structures serve to compartmentalize the lumen of peroxisomes thereby preventing interference of biochemical reactions. Metabolic compartmentalization of peroxisomes via assembly of specific proteins may occur in other organisms as well.

• Nähse, Viola; Stenmark, Harald Alfred & Schink, Kay Oliver (2024). Omegasomes control formation, expansion, and closure of autophagosomes. Bioessays. ISSN 0265-9247. 46(6). doi: 10.1002/bies.202400038. Full text in Research Archive Show summary

  Autophagy, an essential cellular process for maintaining cellular homeostasis and eliminating harmful cytoplasmic objects, involves the de novo formation of double-membraned autophagosomes that engulf and degrade cellular debris, protein aggregates, damaged organelles, and pathogens. Central to this process is the phagophore, which forms from donor membranes rich in lipids synthesized at various cellular sites, including the endoplasmic reticulum (ER), which has emerged as a primary source. The ER-associated omegasomes, characterized by their distinctive omega-shaped structure and accumulation of phosphatidylinositol 3-phosphate (PI3P), play a pivotal role in autophagosome formation. Omegasomes are thought to serve as platforms for phagophore assembly by recruiting essential proteins such as DFCP1/ZFYVE1 and facilitating lipid transfer to expand the phagophore. Despite the critical importance of phagophore biogenesis, many aspects remain poorly understood, particularly the complete range of proteins involved in omegasome dynamics, and the detailed mechanisms of lipid transfer and membrane contact site formation.

• Nähse, Viola; Schink, Kay Oliver & Stenmark, Harald Alfred (2023). ATPase-regulated autophagosome biogenesis. Autophagy. ISSN 1554-8627. 20(1), p. 218–219. doi: 10.1080/15548627.2023.2255967. Full text in Research Archive Show summary

  Omega-shaped domains of the endoplasmic reticulum, known as omegasomes, have been suggested to contribute to autophagosome biogenesis, although their exact function is not known. Omegasomes are characterized by the presence of the double FYVE domain containing protein ZFYVE1/DFCP1, but it has remained a paradox that depletion of ZFYVE1 does not prevent bulk macroautophagy/autophagy. We recently showed that ZFYVE1 contains an N-terminal ATPase domain which dimerizes upon ATP binding. Mutations in the ATPase domain that inhibit ATP binding or hydrolysis do not prevent omegasome expansion and maturation. However, omegasome constriction is inhibited by these mutations, which results in an increased lifetime and thereby higher number of omegasomes. Interestingly, whereas ZFYVE1 knockout or mutations do not significantly affect bulk autophagy, selective autophagy of mitochondria, protein aggregates and micronuclei is inhibited. We propose that ATP binding and hydrolysis control the di- or multimerization state of ZFYVE1 which could provide the mechanochemical energy to drive large omegasome constriction and autophagosome completion.

• Raiborg, Camilla; Tan, Kia Wee; Mørk, Sissel; Torgersen, Maria Lyngaas; Wenzel, Eva & Grifo, Mireia Nager [Show all 12 contributors for this article] (2023). ATPase activity of DFCP1 controls selective autophagy. Nature Communications. 14(1). doi: 10.1038/s41467-023-39641-9. Full text in Research Archive Show summary

  Cellular homeostasis is governed by removal of damaged organelles and protein aggregates by selective autophagy mediated by cargo adaptors such as p62/SQSTM1. Autophagosomes can assemble in specialized cup-shaped regions of the endoplasmic reticulum (ER) known as omegasomes, which are characterized by the presence of the ER protein DFCP1/ZFYVE1. The function of DFCP1 is unknown, as are the mechanisms of omegasome formation and constriction. Here, we demonstrate that DFCP1 is an ATPase that is activated by membrane binding and dimerizes in an ATP-dependent fashion. Whereas depletion of DFCP1 has a minor effect on bulk autophagic flux, DFCP1 is required to maintain the autophagic flux of p62 under both fed and starved conditions, and this is dependent on its ability to bind and hydrolyse ATP. While DFCP1 mutants defective in ATP binding or hydrolysis localize to forming omegasomes, these omegasomes fail to constrict properly in a size-dependent manner. Consequently, the release of nascent autophagosomes from large omegasomes is markedly delayed. While knockout of DFCP1 does not affect bulk autophagy, it inhibits selective autophagy, including aggrephagy, mitophagy and micronucleophagy. We conclude that DFCP1 mediates ATPase-driven constriction of large omegasomes to release autophagosomes for selective autophagy.

• Frikstad, Kari-Anne; Schink, Kay Oliver; Gilani, Sania; Pedersen, Lotte B. & Patzke, Sebastian (2022). 3D-Structured Illumination Microscopy of Centrosomes in Human Cell Lines. Bio-protocol. 12(6). doi: 10.21769/BioProtoc.4360. Full text in Research Archive
• Nähse, Viola; Tan, Kia Wee; Campsteijn, Coen; Brech, Andreas; Schink, Kay Oliver & Stenmark, Harald (2021). JIP4 is recruited by the phosphoinositide-binding protein Phafin2 to promote recycling tubules on macropinosomes. Journal of Cell Science. ISSN 0021-9533. 134(14), p. 1–15. doi: 10.1242/jcs.258495. Full text in Research Archive Show summary

  ABSTRACT Macropinocytosis allows cells to take up extracellular material in a non-selective manner into large vesicles called macropinosomes. After internalization, macropinosomes acquire phosphatidylinositol 3-phosphate (PtdIns3P) on their limiting membrane as they mature into endosomal-like vesicles. The molecular mechanisms that underlie recycling of membranes and transmembrane proteins from these macropinosomes still need to be defined. Here, we report that JIP4 (officially known as SPAG9), a protein previously described to bind to microtubule motors, is recruited to tubulating subdomains on macropinosomes by the PtdIns3P-binding protein Phafin2 (officially known as PLEKHF2). These JIP4-positive tubulating subdomains on macropinosomes contain F-actin, the retromer recycling complex and the retromer cargo VAMP3. Disruption of the JIP4–Phafin2 interaction, deletion of Phafin2 or inhibition of PtdIns3P production by VPS34 impairs JIP4 recruitment to macropinosomes. Whereas knockout of JIP4 suppresses tubulation, its overexpression enhances tubulation from macropinosomes. JIP4-knockout cells display increased retention of macropinocytic cargo in both early and late macropinosomes. Collectively, these data identify JIP4 and Phafin2 as components of a tubular recycling pathway that operates from macropinosomes. This article has an associated First Person interview with the first author of the paper.

• Schink, Kay Oliver; Tan, Kia Wee; Spangenberg, Helene; Martorana, Domenica; Sneeggen, Marte & Stévenin, Virginie [Show all 10 contributors for this article] (2021). The phosphoinositide coincidence detector Phafin2 promotes macropinocytosis by coordinating actin organisation at forming macropinosomes. Nature Communications. 12(1), p. 1–17. doi: 10.1038/s41467-021-26775-x. Full text in Research Archive Show summary

  Abstract Uptake of large volumes of extracellular fluid by actin-dependent macropinocytosis has an important role in infection, immunity and cancer development. A key question is how actin assembly and disassembly are coordinated around macropinosomes to allow them to form and subsequently pass through the dense actin network underlying the plasma membrane to move towards the cell center for maturation. Here we show that the PH and FYVE domain protein Phafin2 is recruited transiently to newly-formed macropinosomes by a mechanism that involves coincidence detection of PtdIns3P and PtdIns4P. Phafin2 also interacts with actin via its PH domain, and recruitment of Phafin2 coincides with actin reorganization around nascent macropinosomes. Moreover, forced relocalization of Phafin2 to the plasma membrane causes rearrangement of the subcortical actin cytoskeleton. Depletion of Phafin2 inhibits macropinosome internalization and maturation and prevents KRAS-transformed cancer cells from utilizing extracellular protein as an amino acid source. We conclude that Phafin2 promotes macropinocytosis by controlling timely delamination of actin from nascent macropinosomes for their navigation through the dense subcortical actin network.

• Zdzalik-Bielecka, Daria; Poswiata, Agata; Kozik, Kamila; Jastrzębski, Kamil; Schink, Kay Oliver & Brewinska-Olchowik, Marta [Show all 9 contributors for this article] (2021). The GAS6-AXL signaling pathway triggers actin remodeling that drives membrane ruffling, macropinocytosis, and cancer-cell invasion. Proceedings of the National Academy of Sciences of the United States of America (PNAS). ISSN 0027-8424. 118(28). doi: 10.1073/pnas.2024596118. Full text in Research Archive
• Anda, Silje; Boye, Erik; Schink, Kay Oliver & Grallert, Beata (2021). Cosegregation of asymmetric features during cell division. Open Biology. 11(8), p. 1–11. doi: 10.1098/rsob.210116. Full text in Research Archive Show summary

  Cellular asymmetry plays a major role in the ageing and evolution of multicellular organisms. However, it remains unknown how the cell distinguishes ‘old’ from ‘new’ and whether asymmetry is an attribute of highly specialized cells or a feature inherent in all cells. Here, we investigate the segregation of three asymmetric features: old and new DNA, the spindle pole body (SPB, the centrosome analogue) and the old and new cell ends, using a simple unicellular eukaryote, Schizosaccharomyces pombe. To our knowledge, this is the first study exploring three asymmetric features in the same cells. We show that of the three chromosomes of S. pombe, chromosome I containing the new parental strand, preferentially segregated to the cells inheriting the old cell end. Furthermore, the new SPB also preferentially segregated to the cells inheriting the old end. Our results suggest that the ability to distinguish ‘old’ from ‘new’ and to segregate DNA asymmetrically are inherent features even in simple unicellular eukaryotes.

• Palušová, Veronika; Renzová, Tereza; Verlande, Amandine; Vaclová, Tereza; Medková, Michaela & Cetlová, Linda [Show all 19 contributors for this article] (2020). Dual targeting of BRAF and mTOR signaling in melanoma cells with pyridinyl imidazole compounds. Cancers. 12(6), p. 1–24. doi: 10.3390/cancers12061516. Full text in Research Archive Show summary

  BRAF inhibitors can delay the progression of metastatic melanoma, but resistance usually emerges, leading to relapse. Drugs simultaneously targeting two or more pathways essential for cancer growth could slow or prevent the development of resistant clones. Here, we identified pyridinyl imidazole compounds SB202190, SB203580, and SB590885 as dual inhibitors of critical proliferative pathways in human melanoma cells bearing the V600E activating mutation of BRAF kinase. We found that the drugs simultaneously disrupt the BRAF V600E-driven extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK) activity and the mechanistic target of rapamycin complex 1 (mTORC1) signaling in melanoma cells. Pyridinyl imidazole compounds directly inhibit BRAF V600E kinase. Moreover, they interfere with the endolysosomal compartment, promoting the accumulation of large acidic vacuole-like vesicles and dynamic changes in mTOR signaling. A transient increase in mTORC1 activity is followed by the enrichment of the Ragulator complex protein p18/LAMTOR1 at contact sites of large vesicles and delocalization of mTOR from the lysosomes. The induced disruption of the endolysosomal pathway not only disrupts mTORC1 signaling, but also renders melanoma cells sensitive to endoplasmic reticulum (ER) stress. Our findings identify new activities of pharmacologically relevant small molecule compounds and provide a biological rationale for the development of anti-melanoma therapeutics based on the pyridinyl imidazole core.

• Sneeggen, Marte; Schink, Kay Oliver & Stenmark, Harald (2019). Tumor suppression by control of matrix metalloproteinase recycling. Molecular and Cellular Oncology (MCO). 6(6), p. 1–3. doi: 10.1080/23723556.2019.1646606. Full text in Research Archive Show summary

  Secretion of matrix metalloproteinases (MMPs) enables cancer cells to degrade extracellular matrix, thus promoting tumor invasion and metastasis. We have recently found that the endosomal protein WDFY2 serves as a gatekeeper for MMP recycling from endosomes and that deletion of WDFY2, which is frequently lost in metastatic cancers, causes increased matrix degradation and cell invasion.

• Frikstad, Kari-Anne; Molinari, Elisa; Thoresen, Marianne; Ramsbottom, Simon A; Hughes, Frances & Letteboer, Stef J.F. [Show all 16 contributors for this article] (2019). A CEP104-CSPP1 Complex Is Required for Formation of Primary Cilia Competent in Hedgehog Signaling. Cell reports. 28(7), p. 1907–1922.e6. doi: 10.1016/j.celrep.2019.07.025. Full text in Research Archive
• Ackermann, Frauke; Schink, Kay Oliver; Bruns, Christine; Izsvàk, Zsuzsanna; Hamra, F. Kent & Rosenmund, Christian [Show all 7 contributors for this article] (2019). Critical role for Piccolo in synaptic vesicle retrieval. eLIFE. 8. doi: 10.7554/eLife.46629. Full text in Research Archive
• Zhen, Yan; Spangenberg, Helene; Munson, Michael Joseph; Brech, Andreas; Schink, Kay Oliver & Tan, Kia Wee [Show all 13 contributors for this article] (2019). ESCRT-mediated phagophore sealing during mitophagy. Autophagy. ISSN 1554-8627. p. 1–16. doi: 10.1080/15548627.2019.1639301. Full text in Research Archive Show summary

  Inactivation of the endosomal sorting complex required for transport (ESCRT) machinery has been reported to cause autophagic defects, but the exact functions of ESCRT proteins in macroautophagy/autophagy remain incompletely understood. Using live-cell fluorescence microscopy we found that the filament-forming ESCRT-III subunit CHMP4B was recruited transiently to nascent autophagosomes during starvation-induced autophagy and mitophagy, with residence times of about 1 and 2 min, respectively. Correlative light microscopy and electron tomography revealed CHMP4B recruitment at a late step in mitophagosome formation. The autophagosomal dwell time of CHMP4B was strongly increased by depletion of the regulatory ESCRT-III subunit CHMP2A. Using a novel optogenetic closure assay we observed that depletion of CHMP2A inhibited phagophore sealing during mitophagy. Consistent with this, depletion of CHMP2A and other ESCRT-III subunits inhibited both PRKN/PARKIN-dependent and -independent mitophagy. We conclude that the ESCRT machinery mediates phagophore closure, and that this is essential for mitophagic flux.

• Sneeggen, Marte; Pedersen, Nina Marie; Campsteijn, Coen; Haugsten, Ellen Margrethe; Stenmark, Harald & Schink, Kay Oliver (2019). WDFY2 restrains matrix metalloproteinase secretion and cell invasion by controlling VAMP3-dependent recycling. Nature Communications. 10(1), p. 1–20. doi: 10.1038/s41467-019-10794-w. Full text in Research Archive Show summary

  Cancer cells secrete matrix metalloproteinases to remodel the extracellular matrix, which enables them to overcome tissue barriers and form metastases. The membrane-bound matrix metalloproteinase MT1-MMP (MMP14) is internalized by endocytosis and recycled in endosomal compartments. It is largely unknown how endosomal sorting and recycling of MT1-MMP are controlled. Here, we show that the endosomal protein WDFY2 controls the recycling of MT1-MMP. WDFY2 localizes to endosomal tubules by binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns3P). We identify the v-SNARE VAMP3 as an interaction partner of WDFY2. WDFY2 knockout causes a strong redistribution of VAMP3 into small vesicles near the plasma membrane. This is accompanied by increased, VAMP3-dependent secretion of MT1-MMP, enhanced degradation of extracellular matrix, and increased cell invasion. WDFY2 is frequently lost in metastatic cancers, most predominantly in ovarian and prostate cancer. We propose that WDFY2 acts as a tumor suppressor by serving as a gatekeeper for VAMP3 recycling.

• Theodossiou, Theodossis; Ali, Muhammad; Grigalavicius, Mantas; Grallert, Beata; Dillard, Pierre & Schink, Kay Oliver [Show all 12 contributors for this article] (2019). Simultaneous defeat of MCF7 and MDA-MB-231 resistances by a hypericin PDT-tamoxifen hybrid therapy. NPJ breast cancer. doi: 10.1038/s41523-019-0108-8. Full text in Research Archive
• Wenzel, Eva; Schultz, Sebastian; Schink, Kay Oliver; Pedersen, Nina Marie; Nähse, Viola & Carlson, Andreas [Show all 9 contributors for this article] (2018). Concerted ESCRT and clathrin recruitment waves define the timing and morphology of intraluminal vesicle formation. Nature Communications. 9(2932), p. 1–18. doi: 10.1038/s41467-018-05345-8. Full text in Research Archive Show summary

  The endosomal sorting complex required for transport (ESCRT) machinery mediates cargo sorting, membrane deformation and membrane scission on the surface of endosomes, generating intraluminal vesicles (ILVs) to degrade signaling receptors. By live-cell imaging of individual endosomes in human cells, we find that ESCRT proteins are recruited in a repetitive pattern: ESCRT-0 and -I show a gradual and linear recruitment and dissociation, whereas ESCRT-III and its regulatory ATPase VPS4 display fast and transient dynamics. Electron microscopy shows that ILVs are formed consecutively, starting immediately after endocytic uptake of cargo proteins and correlating with the repeated ESCRT recruitment waves, unraveling the timing of ILV formation. Clathrin, recruited by ESCRT-0, is required for timely ESCRT-0 dissociation, efficient ILV formation, correct ILV size and cargo degradation. Thus, cargo sorting and ILV formation occur by concerted, coordinated and repetitive recruitment waves of individual ESCRT subcomplexes and are controlled by clathrin.

• Radulovic, Maja; Schink, Kay Oliver; Wenzel, Eva; Nähse, Viola; Bongiovanni, Antonino & Lafont, Frank [Show all 7 contributors for this article] (2018). ESCRT-mediated lysosome repair precedes lysophagy and promotes cell survival. EMBO Journal. ISSN 0261-4189. 37:e00753, p. 1–15. doi: 10.15252/embj.201899753. Full text in Research Archive Show summary

  Although lysosomes perform a number of essential cellular functions, damaged lysosomes represent a potential hazard to the cell. Such lysosomes are therefore engulfed by autophagic membranes in the process known as lysophagy, which is initiated by recognition of luminal glycoprotein domains by cytosolic lectins such as Galectin‐3. Here, we show that, under various conditions that cause injury to the lysosome membrane, components of the endosomal sorting complex required for transport (ESCRT)‐I, ESCRT‐II, and ESCRT‐III are recruited. This recruitment occurs before that of Galectin‐3 and the lysophagy machinery. Subunits of the ESCRT‐III complex show a particularly prominent recruitment, which depends on the ESCRT‐I component TSG101 and the TSG101‐ and ESCRT‐III‐binding protein ALIX. Interference with ESCRT recruitment abolishes lysosome repair and causes otherwise reversible lysosome damage to become cell lethal. Vacuoles containing the intracellular pathogen Coxiella burnetii show reversible ESCRT recruitment, and interference with this recruitment reduces intravacuolar bacterial replication. We conclude that the cell is equipped with an endogenous mechanism for lysosome repair which protects against lysosomal damage‐induced cell death but which also provides a potential advantage for intracellular pathogens.

• Lång, Anna Ulrika; Eriksson, Jens; Schink, Kay Oliver; Lång, Emma Helena; Blicher, Pernille & Polec, Anna [Show all 9 contributors for this article] (2017). Visualization of PML nuclear import complexes reveals FG-repeat nucleoporins at cargo retrieval sites. Nucleus. ISSN 1949-1034. 8(4), p. 404–420. doi: 10.1080/19491034.2017.1306161. Full text in Research Archive
• Raiborg, Camilla; Schink, Kay Oliver & Stenmark, Harald Alfred (2017). Suppressing mTORC1 on the lysosome. EMBO Journal. ISSN 0261-4189. 36(13), p. 1803–1991. doi: 10.15252/embj.201797469. Full text in Research Archive
• Fosdahl, Anne Marthe; Dietrich, Markus; Schink, Kay Oliver; Malik, Muhammad Salman; Skeie, Marianne & Bertelsen, Vibeke [Show all 7 contributors for this article] (2017). ErbB3 interacts with Hrs and is sorted to lysosomes for degradation. BBA - Molecular Cell Research. ISSN 0167-4889. 1864(12), p. 2241–2252. doi: 10.1016/j.bbamcr.2017.08.011. Full text in Research Archive
• Katheder, Nadja Sandra; Khezri, Rojyar; O'Farrell, Fergal; Schultz, Sebastian; Jain, Ashish & Rahman, Mohammed Mahidur [Show all 14 contributors for this article] (2017). Microenvironmental autophagy promotes tumour growth. Nature. ISSN 0028-0836. 541(7637), p. 417–420. doi: 10.1038/nature20815. Full text in Research Archive
• Schink, Kay Oliver; Tan, Kia Wee & Stenmark, Harald Alfred (2016). Phosphoinositides in Control of Membrane Dynamics. Annual Review of Cell and Developmental Biology. ISSN 1081-0706. 32, p. 143–171. doi: 10.1146/annurev-cellbio-111315-125349. Full text in Research Archive
• Helgesen, Emily; Fossum-Raunehaug, Solveig; Sætre, Frank; Schink, Kay Oliver & Skarstad, Kirsten Jane (2015). Dynamic Escherichia coli SeqA complexes organize the newly replicated DNA at a considerable distance from the replisome. Nucleic Acids Research (NAR). ISSN 0305-1048. 43(5), p. 2730–2743. doi: 10.1093/nar/gkv146. Full text in Research Archive
• Vietri, Marina; Schink, Kay Oliver; Campsteijn, Coen; Wegner, Catherine E Sem; Schultz, Sebastian & Christ, Liliane Florence [Show all 10 contributors for this article] (2015). Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. Nature. ISSN 0028-0836. 522(7555), p. 231–235. doi: 10.1038/nature14408. Full text in Research Archive
• Sternemalm, Anders Johan Wilhelm; Geimer, Stefan; Frikstad, Kari-Anne; Schink, Kay Oliver; Stokke, Trond & Patzke, Sebastian (2015). CSPP-L associates with the desmosome of polarized epithelial cells and is required for normal spheroid formation. PLOS ONE. 10:e0134789(8). doi: 10.1371/journal.pone.0134789. Full text in Research Archive
• Raiborg, Camilla; Wenzel, Eva; Pedersen, Nina Marie; Olsvik, Hallvard Lauritz; Schink, Kay Oliver & Schultz, Sebastian [Show all 12 contributors for this article] (2015). Repeated ER-endosome contacts promote endosome translocation and neurite outgrowth. Nature. ISSN 0028-0836. 520(7546), p. 234–238. doi: 10.1038/nature14359. Full text in Research Archive
• Drießen, Stefan; Berleth, Niklas; Friesen, Olena; Löffler, Antje S.; Böhler, Philip & Hieke, Nora [Show all 15 contributors for this article] (2015). Deubiquitinase inhibition by WP1130 leads to ULK1 aggregation and blockade of autophagy. Autophagy. ISSN 1554-8627. 11(9), p. 1458–1470. doi: 10.1080/15548627.2015.1067359. Full text in Research Archive
• Palibrk, Vuk; Lång, Emma Helena; Lång, Anna Ulrika; Schink, Kay Oliver; Rowe, Alexander D. & Bøe, Stig Ove (2014). Promyelocytic leukemia bodies tether to early endosomes during mitosis. Cell Cycle. ISSN 1538-4101. 13(11), p. 1749–1755. doi: 10.4161/cc.28653. Full text in Research Archive
• Oeste, Clara L.; Pinar, Mario; Schink, Kay Oliver; Martínez-Turrión, Javier; Stenmark, Harald & Peñalva, Miguel A. [Show all 7 contributors for this article] (2014). An Isoprenylation and Palmitoylation Motif Promotes Intraluminal Vesicle Delivery of Proteins in Cells from Distant Species. PLOS ONE. 9:00107190(9). doi: 10.1371/journal.pone.0107190. Full text in Research Archive
• Stiebler, Alina C.; Freitag, Johannes; Schink, Kay Oliver; Stehlik, Thorsten; Tillmann, Britta A.M. & Ast, Julia [Show all 7 contributors for this article] (2014). Ribosomal Readthrough at a Short UGA Stop Codon Context Triggers Dual Localization of Metabolic Enzymes in Fungi and Animals. PLoS Genetics. ISSN 1553-7390. 10(10). doi: 10.1371/journal.pgen.1004685. Full text in Research Archive
• Wegner, Catherine E Sem; Schink, Kay Oliver; Stenmark, Harald Alfred & Brech, Andreas (2014). Monitoring phosphatidylinositol 3-phosphate in multivesicular endosome biogenesis. Methods in Enzymology. ISSN 0076-6879. 534, p. 3–23. doi: 10.1016/B978-0-12-397926-1.00001-9. Full text in Research Archive
• Thoresen, Sigrid Bratlie; Campsteijn, Coen; Vietri, Marina; Schink, Kay Oliver; Liestøl, Knut & Andersen, Jens S. [Show all 8 contributors for this article] (2014). ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4. Nature Cell Biology. ISSN 1465-7392. 16(6), p. 547–557. doi: 10.1038/ncb2959. Full text in Research Archive
• Oppelt, Angela; Lobert, Viola Helene; Haglund, Kaisa; Mackey, Ashley M.; Rameh, Lucia E. & Liestøl, Knut [Show all 14 contributors for this article] (2013). Production of phosphatidylinositol 5-phosphate via PIKfyve and MTMR3 regulates cell migration. EMBO Reports. ISSN 1469-221X. 14(1), p. 57–64. doi: 10.1038/embor.2012.183. Full text in Research Archive
• Schink, Kay Oliver; Raiborg, Camilla & Stenmark, Harald Alfred (2013). Phosphatidylinositol 3-phosphate, a lipid that regulates membrane dynamics, protein sorting and cell signalling. Bioessays. ISSN 0265-9247. 35(10), p. 900–912. doi: 10.1002/bies.201300064. Full text in Research Archive
• Raiborg, Camilla; Schink, Kay Oliver & Stenmark, Harald Alfred (2013). ClassIII phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic. The FEBS Journal. ISSN 1742-464X. 280(12), p. 2730–2742. doi: 10.1111/febs.12116. Full text in Research Archive
• Fykerud, Tone; Kjenseth, Ane Hansen; Schink, Kay Oliver; Sirnes, Solveig; Bruun, Jarle & Omori, Yasufumi [Show all 9 contributors for this article] (2012). Smad ubiquitination regulatory factor-2 controls gap junction intercellular communication by modulating endocytosis and degradation of connexin43. Journal of Cell Science. ISSN 0021-9533. 125(17), p. 3966–3976. doi: 10.1242/jcs.093500. Full text in Research Archive
• Freitag, Johannes; Lanver, Daniel; Böhmer, Christian; Schink, Kay Oliver; Bölker, Michael & Sandrock, Björn (2011). Septation of Infectious Hyphae Is Critical for Appressoria Formation and Virulence in the Smut Fungus Ustilago Maydis. PLoS Pathogens. ISSN 1553-7366. 7(5). doi: 10.1371/journal.ppat.1002044. Full text in Research Archive
• Nezis, Ioannis; Sagona, Antonia; Schink, Kay Oliver & Stenmark, Harald Alfred (2010). Divide and ProsPer: The emerging role of PtdIns3P in cytokinesis. Trends in Cell Biology. ISSN 0962-8924. 20(11), p. 642–649. doi: 10.1016/j.tcb.2010.08.010. Full text in Research Archive
• Stuffers, Susanne; Malerød, Lene; Schink, Kay Oliver; Corvera, Silvia; Stenmark, Harald Alfred & Brech, Andreas (2010). Time-resolved Ultrastructural Detection of Phosphatidylinositol 3-phosphate. Journal of Histochemistry and Cytochemistry. ISSN 0022-1554. 14(42), p. 1025–1032. doi: 10.1369/jhc.2010.955815. Full text in Research Archive

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• Mierke, Claudia Tanja; Hu, Xian; Yao, Mingxi; Schink, Kay Oliver & Sheetz, Michael (2024). Editorial: Tumor cell mechanosensitivity: molecular basis. Frontiers in Cell and Developmental Biology. 12. doi: 10.3389/fcell.2024.1484725. Full text in Research Archive
• Grøvdal, Lene Melsæther; Schink, Kay Oliver; Pelka, Karin; Husebye, Harald; Latz, Eicke & Stenmark, Harald Alfred [Show all 7 contributors for this article] (2016). Moving Tolls - Novel interactors of TLR9 trafficking. Full text in Research Archive
• Grøvdal, Lene Melsæther; Schink, Kay Oliver; Pelka, Karin; Husebye, Harald; Latz, Eicke & Stenmark, Harald Alfred [Show all 7 contributors for this article] (2016). Moving Tolls - novel interactors of TLR9 trafficking. Full text in Research Archive
• Grøvdal, Lene Melsæther; Schink, Kay Oliver; Pelka, Karin; Husebye, Harald; Latz, Eicke & Stenmark, Harald Alfred [Show all 7 contributors for this article] (2015). Moving Tolls - novel interactors of TLR9 trafficking. Full text in Research Archive
• Grøvdal, Lene Melsæther; Schink, Kay Oliver; Pelka, Karin; Husebye, Harald; Latz, Eicke & Stenmark, Harald Alfred [Show all 7 contributors for this article] (2015). Moving Tolls - novel interactors of TLR9 trafficking. Full text in Research Archive
• Schink, Kay Oliver & Stenmark, Harald Alfred (2011). Cell Differentiation: Midbody Remnants - Junk or Fate Factors? Current Biology. ISSN 0960-9822. 21(23), p. R958–R960. Full text in Research Archive

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