Jørgen Wesche

• 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
• Song, Linlin; Kostas, Michal Janusz; Lærdahl, Jon Kristen; Skálová, Marie; Janská, Tereza & Juzeniene, Asta [Show all 14 contributors for this article] (2025). Preparation and Characterization of an Engineered FGF1 Conjugated to 161 Tb for Targeting of FGFRs. ACS Omega. 10(6), p. 5730–5743. doi: 10.1021/acsomega.4c09179. Full text in Research Archive Show summary

  The fibroblast growth factor receptor family members, FGFR1-4, are frequently overexpressed in various solid tumors, including breast cancer and sarcomas. This overexpression highlights the potential of the family of FGFRs as promising targets for cancer therapy. However, conventional FGFR kinase inhibitors often encounter challenges such as limited efficacy or drug resistance. In this study, we pursue an alternative strategy by designing a conjugate of the FGFR ligand FGF1 with the radioisotope 161Tb, for targeted therapy in FGFR-overexpressing cancer cells. FGF1 was engineered (eFGF1) to incorporate a single cysteine at the C terminus for site-specific labeling with a DOTA chelator. eFGF1-DOTA was mixed with the radioisotope 161Tb under mild conditions, resulting in a labeling efficiency above 90%. The nonradioactive ligands were characterized by mass spectrometry, while radioligands were characterized by thin-layer chromatography. The targeting function of the radioligands was assessed through confocal microscopy, flow cytometry, and Western blot analysis, focusing on binding to cancer cells and the activation of downstream signaling pathways related to FGFR. When compared to MCF-7 and RD cell lines with low FGFR expression, eFGF1-DOTA-Tb[161Tb] radioligands demonstrated significantly higher accumulation in FGFR-overexpressing cell lines (MCF-7 FGFR1 and RMS559), leading to enhanced cytotoxicity. Besides radionuclides, eFGF1 can also deliver doxorubicin (DOX) into cancer cells. Considering these characteristics, eFGF1-DOTA-Tb[161Tb] and eFGF1-DOX emerge as promising candidates for FGFR-targeted cancer therapy, and further evaluation in vivo is warranted.

• Bjørnerud, Birgitte; Wesche, Jørgen & Haugsten, Ellen Margrethe (2025). A rhabdomyosarcoma cell migration inhibitor screen using phase-contrast microscopy. Experimental Cell Research. ISSN 0014-4827. 449(1). doi: 10.1016/j.yexcr.2025.114582. Full text in Research Archive Show summary

  Rhabdomyosarcoma (RMS) is a malignant soft tissue tumour occurring in young children. Alterations in fibroblast growth factor receptor 4 (FGFR4) signalling pathways are linked to metastasis and poor prognosis in RMS. A critical trait of metastatic disease is the ability of cancer cells to migrate and invade nearby and distant tissues. To study cell migration, we have developed a computational tool that automatically tracks and measures the velocity of migrating cells in phase contrast images. This tool facilitated an inhibitor screen comprising 462 compounds, analysing nearly 2000 videos and tracking approximately 700 000 RMS-derived cells harbouring a constitutively active FGFR4 (RMS559). The highly selective inhibitor screen targeted various signalling pathways, including receptor tyrosine kinases (RTKs), mitogen-activated protein kinases (MAPK), and phosphoinositide 3-kinases (PI3K). Validation of screen hits revealed that inhibiting proteins in the MAPK and PI3K pathway decreased cell migration and, in some cases, cell viability. Inhibiting FGFR4 resulted in decreased RMS559 cell migration, while, surprisingly, inhibitors targeting Rho-associated protein kinase (ROCK) and focal adhesion kinase (FAK) resulted in increased RMS559 cell migration. Mechanistically, the inhibition of ROCK and FAK resulted in fewer focal adhesions, thereby facilitating increased cell velocity. These findings suggest that targeting specific signalling pathways can effectively modulate migration and survival of metastatic RMS559 cells.

• Nakken, Sigve; Gundersen, Sveinung; Bernal, Fabian Leonardo Martinez; Polychronopoulos, Dimitris; Hovig, Eivind & Wesche, Jørgen (2023). Comprehensive interrogation of gene lists from genome-scale cancer screens with oncoEnrichR. International Journal of Cancer. ISSN 0020-7136. 153(10), p. 1819–1828. doi: 10.1002/ijc.34666. Full text in Research Archive Show summary

  Genome-scale screening experiments in cancer produce long lists of candidate genes that require extensive interpretation for biological insight and prioritization for follow-up studies. Interrogation of gene lists frequently represents a significant and time-consuming undertaking, in which experimental biologists typically combine results from a variety of bioinformatics resources in an attempt to portray and understand cancer relevance. As a means to simplify and strengthen the support for this endeavor, we have developed oncoEnrichR, a flexible bioinformatics tool that allows cancer researchers to comprehensively interrogate a given gene list along multiple facets of cancer relevance. oncoEnrichR differs from general gene set analysis frameworks through the integration of an extensive set of prior knowledge specifically relevant for cancer, including ranked gene-tumor type associations, literature-supported proto-oncogene and tumor suppressor gene annotations, target druggability data, regulatory interactions, synthetic lethality predictions, as well as prognostic associations, gene aberrations and co-expression patterns across tumor types. The software produces a structured and user-friendly analysis report as its main output, where versions of all underlying data resources are explicitly logged, the latter being a critical component for reproducible science. We demonstrate the usefulness of oncoEnrichR through interrogation of two candidate lists from proteomic and CRISPR screens. oncoEnrichR is freely available as a web-based service hosted by the Galaxy platform (https://oncotools.elixir.no), and can also be accessed as a stand-alone R package (https://github.com/sigven/oncoEnrichR).

• Holme, Børge; Bjørnerud, Birgitte; Pedersen, Nina Marie; Ballina, Laura Rodriguez de la; Wesche, Jørgen & Haugsten, Ellen Margrethe (2023). Automated tracking of cell migration in phase contrast images with CellTraxx. Scientific Reports. 13(1). doi: 10.1038/s41598-023-50227-9. Full text in Research Archive Show summary

  The ability of cells to move and migrate is required during development, but also in the adult in processes such as wound healing and immune responses. In addition, cancer cells exploit the cells’ ability to migrate and invade to spread into nearby tissue and eventually metastasize. The majority of cancer deaths are caused by metastasis and the process of cell migration is therefore intensively studied. A common way to study cell migration is to observe cells through an optical microscope and record their movements over time. However, segmenting and tracking moving cells in phase contrast time-lapse video sequences is a challenging task. Several tools to track the velocity of migrating cells have been developed. Unfortunately, most of the automated tools are made for fluorescence images even though unlabelled cells are often preferred to avoid phototoxicity. Consequently, researchers are constrained with laborious manual tracking tools using ImageJ or similar software. We have therefore developed a freely available, user-friendly, automated tracking tool called CellTraxx. This software makes it easy to measure the velocity and directness of migrating cells in phase contrast images. Here, we demonstrate that our tool efficiently recognizes and tracks unlabelled cells of different morphologies and sizes (HeLa, RPE1, MDA-MB-231, HT1080, U2OS, PC-3) in several types of cell migration assays (random migration, wound healing and cells embedded in collagen). We also provide a detailed protocol and download instructions for CellTraxx.

• Fiorito, Elisa; Szybowska, Patrycja Maria; Haugsten, Ellen Margrethe; Kostas, Michal Janusz; Øy, Geir Frode & Wiedlocha, Antoni [Show all 12 contributors for this article] (2022). Strategies to inhibit FGFR4 V550L-driven rhabdomyosarcoma. British Journal of Cancer. ISSN 0007-0920. 127, p. 1939–1953. doi: 10.1038/s41416-022-01973-6. Full text in Research Archive Show summary

  Background: Rhabdomyosarcoma (RMS) is a paediatric cancer driven either by fusion proteins (e.g., PAX3-FOXO1) or by mutations in key signalling molecules (e.g., RAS or FGFR4). Despite the latter providing opportunities for precision medicine approaches in RMS, there are currently no such treatments implemented in the clinic.<p> <p>Methods: We evaluated biologic properties and targeting strategies for the FGFR4 V550L activating mutation in RMS559 cells, which have a high allelic fraction of this mutation and are oncogenically dependent on FGFR4 signalling. Signalling and trafficking of FGFR4 V550L were characterised by confocal microscopy and proteomics. Drug effects were determined by live-cell imaging, MTS assay, and in a mouse model. <p>Results: Among recently developed FGFR4-specific inhibitors, FGF401 inhibited FGFR4 V550L-dependent signalling and cell proliferation at low nanomolar concentrations. Two other FGFR4 inhibitors, BLU9931 and H3B6527, lacked potent activity against FGFR4 V550L. Alternate targeting strategies were identified by RMS559 phosphoproteomic analyses, demonstrating that RAS/MAPK and PI3K/AKT are essential druggable pathways downstream of FGFR4 V550L. Furthermore, we found that FGFR4 V550L is HSP90- dependent, and HSP90 inhibitors efficiently impeded RMS559 proliferation. In a RMS559 mouse xenograft model, the pan-FGFR inhibitor, LY2874455, did not efficiently inhibit growth, whereas FGF401 potently abrogated growth. <p >Conclusions: Our results pave the way for precision medicine approaches against FGFR4 V550L-driven RMS.

• Munson, Michael Joseph; Mathai, Benan J.; Ng, Matthew; Moncho, Laura Cristina Trachsel; Ballina, Laura R de la & Schultz, Sebastian W. [Show all 13 contributors for this article] (2021). GAK and PRKCD are positive regulators of PRKN-independent mitophagy. Nature Communications. 12(1). doi: 10.1038/s41467-021-26331-7. Full text in Research Archive Show summary

  The mechanisms involved in programmed or damage-induced removal of mitochondria by mitophagy remains elusive. Here, we have screened for regulators of PRKN-independent mitophagy using an siRNA library targeting 197 proteins containing lipid interacting domains. We identify Cyclin G-associated kinase (GAK) and Protein Kinase C Delta (PRKCD) as regulators of PRKN-independent mitophagy, with both being dispensable for PRKN- dependent mitophagy and starvation-induced autophagy. We demonstrate that the kinase activity of both GAK and PRKCD are required for efficient mitophagy in vitro, that PRKCD is present on mitochondria, and that PRKCD facilitates recruitment of ULK1/ATG13 to early autophagic structures. Importantly, we demonstrate in vivo relevance for both kinases in the regulation of basal mitophagy. Knockdown of GAK homologue (gakh-1) in C. elegans or knockout of PRKCD homologues in zebrafish led to significant inhibition of basal mitophagy, highlighting the evolutionary relevance of these kinases in mitophagy regulation.

• Vikan, Aurora; Haugsten, Ellen Margrethe; Kostas, Michal Janusz; Selbo, Pål Kristian & Wesche, Jørgen (2021). Efficacy and selectivity of FGF2-saporin cytosolically delivered by PCI in cells overexpressing fgfr1. Cells. 10(6), p. 1–16. doi: 10.3390/cells10061476. Full text in Research Archive Show summary

  Fibroblast growth factor receptors (FGFRs) have become an attractive target in cancer research and therapy due to their implication in several cancers. Limitations of current treatment options require a need for additional, more specific and potent strategies to overcome cancers driven by FGFRs. Photochemical internalization (PCI) is a light-controlled method for cytosolic delivery of drugs that are entrapped in endosomes and lysosomes. We here evaluated the efficacy and selectivity of PCI of FGF2-saporin (FGF-SAP) in cells overexpressing FGFR1. FGF-SAP is a conjugate of FGF2 and the highly cytotoxic ribosome-inactivating protein (RIP) saporin, which is used as payload to eliminate cancer cells. Evaluation of the targeting effect of PCI of FGF-SAP was done by comparing the cytotoxic response in osteosarcoma cells with very low levels of FGFR1 (U2OS) to cells overexpressing FGFR1 (U2OS-R1). We demonstrate that PCI greatly enhances cytotoxicity of the drug showing efficient cell killing at pM concentrations of the drug in U2OS-R1 cells. However, U2OS cells were also sensitive to the toxin after PCI. Binding experiments using confocal microscopy and Western blotting techniques indicate that FGF-SAP is taken up by cells through heparan sulfate proteoglycans (HSPGs) in U2OS cells. We further show that the cytotoxicity of FGF-SAP in U2OS cells was reduced when cells were co-treated with heparin to compete out binding to HSPG, demonstrating that the cytotoxic effect was due to internalization by HSPGs. We conclude that to prevent off-target effects of FGF-based toxins, it will be necessary to circumvent binding to HSPGs, for example by mutating the binding site of FGF2 to HSPGs.

• Szybowska, Patrycja Maria; Kostas, Michal Janusz; Wesche, Jørgen; Haugsten, Ellen Margrethe & Wiedlocha, Antoni (2021). Negative Regulation of FGFR (Fibroblast Growth Factor Receptor) Signaling. Cells. 10(6), p. 1–18. doi: 10.3390/cells10061342. Full text in Research Archive Show summary

  FGFR (fibroblast growth factor receptor) signaling controls fundamental processes in embryonic, fetal and adult human life. The magnitude, duration, and location of FGFR signaling must be strictly controlled in order to induce the correct biological response. Uncontrolled receptor signaling has been shown to lead to a variety of diseases, such as skeletal disorders and cancer. Here we review the numerous cellular mechanisms that regulate and turn off FGFR signaling, once the receptor is activated. These mechanisms include endocytosis and endocytic sorting, phosphatase activity, negative regulatory proteins and negative feedback phosphorylation events. The mechanisms act together simultaneously or sequentially, controlling the same or different steps in FGFR signaling. Although more work is needed to fully understand the regulation of FGFR signaling, it is clear that the cells in our body have evolved an extensive repertoire of mechanisms that together keep FGFR signaling tightly controlled and prevent excess FGFR signaling.

• Tadele, Dagim Shiferaw; Robertson, Joseph; Crispin, Richard; Herrera, Carmen; Chlubnová, Markéta & Piechaczyk, Laure Isabelle [Show all 14 contributors for this article] (2020). A cell competition-based small molecule screen identifies a novel compound that induces dual c-Myc depletion and p53 activation. Journal of Biological Chemistry. ISSN 0021-9258. 296. doi: 10.1074/jbc.RA120.015285. Full text in Research Archive Show summary

  Breakpoint Cluster Region-Abelson kinase (BCR–Abl) is a driver oncogene that causes chronic myeloid leukemia and a subset of acute lymphoid leukemias. Although tyrosine kinase inhibitors provide an effective treatment for these diseases, they generally do not kill leukemic stem cells (LSCs), the cancer-initiating cells that compete with normal hematopoietic stem cells for the bone marrow niche. New strategies to target cancers driven by BCR–Abl are therefore urgently needed. We performed a small molecule screen based on competition between isogenic untransformed cells and BCR–Abl-transformed cells and identified several compounds that selectively impair the fitness of BCR–Abl-transformed cells. Interestingly, systems-level analysis of one of these novel compounds, DJ34, revealed that it induced depletion of c-Myc and activation of p53. DJ34-mediated c-Myc depletion occurred in a wide range of tumor cell types, including lymphoma, lung, glioblastoma, breast cancer, and several forms of leukemia, with primary LSCs being particularly sensitive to DJ34. Further analyses revealed that DJ34 interferes with c-Myc synthesis at the level of transcription, and we provide data showing that DJ34 is a DNA intercalator and topoisomerase II inhibitor. Physiologically, DJ34 induced apoptosis, cell cycle arrest, and cell differentiation. Taken together, we have identified a novel compound that dually targets c-Myc and p53 in a wide variety of cancers, and with particularly strong activity against LSCs.

• Szybowska, Patrycja Maria; Kostas, Michal Janusz; Wesche, Jørgen; Wiedlocha, Antoni & Haugsten, Ellen Margrethe (2019). Cancer Mutations in FGFR2 Prevent a Negative Feedback Loop Mediated by the ERK1/2 Pathway. Cells. 8(6), p. 1–18. doi: 10.3390/cells8060518. Full text in Research Archive Show summary

  Tight regulation of signaling from receptor tyrosine kinases is required for normal cellular functions and uncontrolled signaling can lead to cancer. Fibroblast growth factor receptor 2 (FGFR2) is a receptor tyrosine kinase that induces proliferation and migration. Deregulation of FGFR2 contributes to tumor progression and activating mutations in FGFR2 are found in several types of cancer. Here, we identified a negative feedback loop regulating FGFR2 signaling. FGFR2 stimulates the Ras/MAPK signaling pathway consisting of Ras-Raf-MEK1/2-ERK1/2. Inhibition of this pathway using a MEK1/2 inhibitor increased FGFR2 signaling. The putative ERK1/2 phosphorylation site at serine 780 (S780) in FGFR2 corresponds to serine 777 in FGFR1 which is directly phosphorylated by ERK1/2. Substitution of S780 in FGFR2 to an alanine also increased signaling. Truncated forms of FGFR2 lacking the C-terminal tail, including S780, have been identified in cancer and S780 has been found mutated to leucine in bladder cancer. Substituting S780 in FGFR2 with leucine increased FGFR2 signaling. Importantly, cells expressing these mutated versions of S780 migrated faster than cells expressing wild-type FGFR2. Thus, ERK1/2-mediated phosphorylation of S780 in FGFR2 constitutes a negative feedback loop and inactivation of this feedback loop in cancer cells causes hyperactivation of FGFR2 signaling, which may result in increased invasive properties.

• Kostas, Michal Janusz; Haugsten, Ellen Margrethe; Zhen, Yan; Sørensen, Vigdis; Szybowska, Patrycja Maria & Fiorito, Elisa [Show all 11 contributors for this article] (2018). Protein Tyrosine Phosphatase Receptor Type G (PTPRG) controls Fibroblast Growth Factor Receptor (FGFR) 1 activity and influences sensitivity to FGFR kinase inhibitors. Molecular & Cellular Proteomics. ISSN 1535-9476. 17(5), p. 850–870. doi: 10.1074/mcp.RA117.000538. Full text in Research Archive Show summary

  Recently, FGFR1 was found to be overexpressed in osteosarcoma and represents an important target for precision medicine. However, because targeted cancer therapy based on FGFR inhibitors has so far been less efficient than expected, a detailed understanding of the target is important. We have here applied proximity-dependent biotin labeling combined with label-free quantitative mass spectrometry to identify determinants of FGFR1 activity in an osteosarcoma cell line. Many known FGFR interactors were identified (e.g. FRS2, PLCG1, RSK2, SRC), but the data also suggested novel determinants. A strong hit in our screen was the tyrosine phosphatase PTPRG. We show that PTPRG and FGFR1 interact and colocalize at the plasma membrane where PTPRG directly dephosphorylates activated FGFR1. We further show that osteosarcoma cell lines depleted for PTPRG display increased FGFR activity and are hypersensitive to stimulation by FGF1. In addition, PTPRG depletion elevated cell growth and negatively affected the efficacy of FGFR kinase inhibitors. Thus, PTPRG may have future clinical relevance by being a predictor of outcome after FGFR inhibitor treatment.

• Zhen, Yan; Haugsten, Ellen Margrethe; Singh, Sachin Kumar & Wesche, Jørgen (2018). Proximity Labeling by a Recombinant APEX2-FGF1 Fusion Protein Reveals Interaction of FGF1 with the Proteoglycans CD44 and CSPG4. Biochemistry. ISSN 0006-2960. 57(26), p. 3807–3816. doi: 10.1021/acs.biochem.8b00120. Full text in Research Archive Show summary

  Fibroblast growth factor 1 (FGF1) binds to specific FGF receptors (FGFRs) at the surface of target cells to initiate intracellular signaling. While heparan sulfate proteoglycans (HSPGs) are well-described coreceptors, it is uncertain whether there are additional binding sites for FGF1 at the cell surface. To address this, we devised and tested a method to identify novel binding sites for FGF1 at the cell surface, which may also be applicable for other protein ligands. We constructed an APEX2–FGF1 fusion protein to perform proximal biotin labeling of proteins following binding of the fusion protein to the cell surface. After functional validation of the fusion protein by a signaling assay, we used this method to identify binding sites for FGF1 on cell surfaces of living cells. We confirmed the feasibility of our approach by detection of FGFR4, a well-known and specific receptor for FGF1. We subsequently screened for novel interactors using RPE1 cells and identified the proteoglycans CSPG4 (NG2) and CD44. We found that FGF1 binds CD44 through its heparin-binding moiety. Moreover, we found that FGF1 was colocalized with both CSPG4 and CD44 at the cell surface, suggesting that these receptors act as storage molecules that create a reservoir of FGF1. Importantly, our data demonstrate that recombinant ligand–APEX2 fusion proteins can be used to identify novel receptor interactions on the cell surface.

• Fafílek, Bohumil; Bálek, Lukáš; Bosakova, Michaela Kunova; Vařecha, Miroslav; Nita, Alexandru & Gregor, Tomas [Show all 20 contributors for this article] (2018). The inositol phosphatase SHIP2 enables sustained ERK activation downstream of FGF receptors by recruiting Src kinases. Science Signaling. ISSN 1945-0877. 11:eaap8608(548), p. 1–15. doi: 10.1126/scisignal.aap8608. Full text in Research Archive Show summary

  Sustained activation of extracellular signal–regulated kinase (ERK) drives pathologies caused by mutations in fibroblast growth factor receptors (FGFRs). We previously identified the inositol phosphatase SHIP2 (also known as INPPL1) as an FGFR-interacting protein and a target of the tyrosine kinase activities of FGFR1, FGFR3, and FGFR4. We report that loss of SHIP2 converted FGF-mediated sustained ERK activation into a transient signal and rescued cell phenotypes triggered by pathologic FGFR-ERK signaling. Mutant forms of SHIP2 lacking phosphoinositide phosphatase activity still associated with FGFRs and did not prevent FGF-induced sustained ERK activation, demonstrating that the adaptor rather than the catalytic activity of SHIP2 was required. SHIP2 recruited Src family kinases to the FGFRs, which promoted FGFR-mediated phosphorylation and assembly of protein complexes that relayed signaling to ERK. SHIP2 interacted with FGFRs, was phosphorylated by active FGFRs, and promoted FGFR-ERK signaling at the level of phosphorylation of the adaptor FRS2 and recruitment of the tyrosine phosphatase PTPN11. Thus, SHIP2 is an essential component of canonical FGF-FGFR signal transduction and a potential therapeutic target in FGFR-related disorders.

• Haugsten, Ellen Margrethe; Sørensen, Vigdis; Bosakova, Michaela Kunova; Souza, Gustavo Antonio De; Krejci, Pavel & Wiedlocha, Antoni [Show all 7 contributors for this article] (2016). Proximity Labeling Reveals Molecular Determinants of FGFR4 Endosomal Transport. Journal of Proteome Research. ISSN 1535-3893. 15(10), p. 3841–3855. doi: 10.1021/acs.jproteome.6b00652. Full text in Research Archive
• Haugsten, Ellen Margrethe; Brech, Andreas; Liestøl, Knut; Norman, Jim C. & Wesche, Jørgen (2014). Photoactivation Approaches Reveal a Role for Rab11 in FGFR4 Recycling and Signalling. Traffic: The moving front of cell biology. ISSN 1398-9219. 15(6), p. 665–683. doi: 10.1111/tra.12168. Full text in Research Archive
• Nadratowska-Wesolowska, Beata; Haugsten, Ellen Margrethe; Zakrzewska, Malgorzata; Jakimowicz, Piotr; Zhen, Yan & Pajdzik, Dorota [Show all 8 contributors for this article] (2014). RSK2 regulates endocytosis of FGF receptor 1 by phosphorylation on serine 789. Oncogene. ISSN 0950-9232. 33(40), p. 4823–4836. doi: 10.1038/onc.2013.425. Full text in Research Archive
• Oppelt, Angela; Haugsten, Ellen Margrethe; Zech, Tobias; Danielsen, Håvard Emil; Sveen, Anita & Lobert, Viola Helene [Show all 8 contributors for this article] (2014). PIKfyve, MTMR3 and their product PtdIns5P regulate cancer cell migration and invasion through activation of Rac1. Biochemical Journal. ISSN 0264-6021. 461(3), p. 383–390. doi: 10.1042/BJ20140132. 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
• Zakrzewska, Malgorzata; Haugsten, Ellen Margrethe; Nadratowska-Wesolowska, Beata; Oppelt, Angela; Hausott, Barbara & Jin, Yixin [Show all 9 contributors for this article] (2013). ERK-Mediated Phosphorylation of Fibroblast Growth Factor Receptor 1 on Ser(777) Inhibits Signaling. Science Signaling. ISSN 1945-0877. 6(262). doi: 10.1126/scisignal.2003087. Full text in Research Archive
• Haugsten, Ellen Margrethe; Oppelt, Angela & Wesche, Jørgen (2013). Phosphatidylinositol 5-phosphate is a second messenger important for cell migration. Communicative & Integrative Biology. 6(5). doi: 10.4161/cib.25446. Full text in Research Archive
• Haugsten, Ellen Margrethe; Zakrzewska, Malgorzata; Brech, Andreas; Pust, Sascha; Olsnes, Sjur & Sandvig, Kirsten [Show all 7 contributors for this article] (2011). Clathrin- and Dynamin-Independent Endocytosis of FGFR3-Implications for Signalling. PLOS ONE. 6(7). doi: 10.1371/journal.pone.0021708. Full text in Research Archive
• Wesche, Jørgen; Haglund, Kaisa & Haugsten, Ellen Margrethe (2011). Fibroblast growth factors and their receptors in cancer. Biochemical Journal. ISSN 0264-6021. 437, p. 199–213. doi: 10.1042/BJ20101603. Full text in Research Archive
• Haglund, Kaisa; Nezis, Jonnis P; Torres, Dafne Lemus; Grabbe, C; Wesche, Jørgen & Liestøl, Knut [Show all 9 contributors for this article] (2010). Cindr Interacts with Anillin to Control Cytokinesis in Drosophila melanogaster. Current Biology. ISSN 0960-9822. 20(10), p. 944–950. doi: 10.1016/j.cub.2010.03.068. Full text in Research Archive
• Lobert, Viola Helene; Brech, Andreas; Pedersen, Nina Marie; Wesche, Jørgen; Oppelt, Angela & Malerød, Lene [Show all 7 contributors for this article] (2010). Ubiquitination of alpha 5 beta 1 lntegrin Controls Fibroblast Migration through Lysosomal Degradation of Fibronectin-lntegrin Complexes. Developmental Cell. ISSN 1534-5807. 19(1), p. 148–159. doi: 10.1016/j.devcel.2010.06.010. Full text in Research Archive
• Haugsten, Ellen Margrethe; Wiedlocha, Antoni; Olsnes, Sjur & Wesche, Jørgen (2010). Roles of Fibroblast Growth Factor Receptors in Carcinogenesis. Molecular Cancer Research. ISSN 1541-7786. 8(11), p. 1439–1452. doi: 10.1158/1541-7786.MCR-10-0168. Full text in Research Archive
• Zakrzewska, Malgorzata; Zhen, Yan; Wiedlocha, Antoni; Olsnes, Sjur & Wesche, Jørgen (2009). Size Limitation in Translocation of Fibroblast Growth Factor 1 Fusion Proteins across the Endosomal Membrane. Biochemistry. ISSN 0006-2960. 48(30), p. 7209–7218. doi: 10.1021/bi9007353. Full text in Research Archive
• Haugsten, Ellen Margrethe; Malecki, Jedrzej M.; Bjørklund, Sunniva Maria Stordal; Olsnes, Sjur & Wesche, Jørgen (2008). Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis. Molecular Biology of the Cell. ISSN 1059-1524. 19, p. 3390–3403. doi: 10.1091/mbc.E07-12-1219. Full text in Research Archive
• Nilsen, Trine; Rosendal, Ken; Sørensen, Vigdis; Wesche, Jørgen; Olsnes, Sjur & Widocha, Antoni (2007). A nuclear export sequence located on a beta-strand in fibroblast growth factor-1. Journal of Biological Chemistry. ISSN 0021-9258. 282(36), p. 26245–26256. doi: 10.1074/jbc.M611234200. Full text in Research Archive
• Wesche, Jørgen; Malecki, Jedrzej M.; Wiedlocha, Antoni; Skjerpen, Camilla Skiple; Claus, P & Olsnes, Sjur (2006). FGF-1 and FGF-2 require the cytosolic chaperone Hsp90 for translocation into the cytosol and the cell nucleus. Journal of Biological Chemistry. ISSN 0021-9258. 281, p. 11405–11412. Full text in Research Archive
• Sørensen, Vigdis; Wiedlocha, Antoni; Haugsten, Ellen Margrethe; Khnykin, Denis; Wesche, Jørgen & Olsnes, Sjur (2006). Different abilities of the four FGFRs to mediate FGF-1 translocation are linked to differences in the receptor C-terminal tail. Journal of Cell Science. ISSN 0021-9533. 119, p. 4332–4341. Full text in Research Archive
• Wiedlocha, Antoni; Nilsen, Trine; Wesche, Jørgen; Sørensen, Vigdis; Malecki, M & Marcinkowska, Ewa [Show all 7 contributors for this article] (2005). Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1. Molecular Biology of the Cell. ISSN 1059-1524. p. 794–810. Full text in Research Archive
• Haugsten, Ellen Margrethe; Sørensen, Vigdis; Olsnes, Sjur; Wesche, Jørgen & Brech, Andreas (2005). Different intracellular trafficking of FGF1 endocytosed by the four specific and homologous FGF receptors. Journal of Cell Science. ISSN 0021-9533. 118, p. 3869–3881. Full text in Research Archive
• Wesche, Jørgen; Malecki, Jedrzej M.; Wiedlocha, Antoni; Ehsani, Maryam; Nilsen, Trine & Marcinkowska, Ewa [Show all 7 contributors for this article] (2005). Two nuclear localization signals required for transport from the cytosol to the, nucleus of externally added FGF-1 translocated into cells. Biochemistry (Moscow). ISSN 0006-2979. 44. Full text in Research Archive
• Malecki, Jedrzej; Wesche, Jørgen; Skjerpen, Camilla Skiple; Wiedlocha, Antoni & Olsnes, Sjur (2004). Translocation of FGF-1 and FGF-2 across Vesicular Membranes Occurs during G1-Phase by a Common Mechanism. Molecular Biology of the Cell. ISSN 1059-1524. 15, p. 804–814. Full text in Research Archive

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• Wesche, Jørgen (2022). Jakten på molekylene som hjelper kreftceller å spre seg til nye steder i kroppen. Full text in Research Archive
• Wesche, Jørgen (2022). Activation of FGFR1 by inorganic phosphate and oxidative stress. Full text in Research Archive
• Skjerpen, Camilla Skiple; Olsnes, Sjur & Wesche, Jørgen (2005). Translocation mechanism and cellular interaction partners of FGF-1 and FGF-2. Universitetet i Oslo. ISSN 9788280721587. Full text in Research Archive

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