anettkd

• Dahl, Anette Kathinka; Mann, Daniel; Lystad, Alf Håkon Lohsen; Sachse, Carsten; Simonsen, Anne Gjøen & Pankiv, Serhiy (2026). Characterizing the membrane recruitment domain of BDCPs and its role in gray platelet syndrome. Journal of Cell Biology. ISSN 0021-9525. 225(10). doi: 10.1083/jcb.202510098. Full text in Research Archive
• Pankiv, Serhiy; Dahl, Anette Kathinka; Aas, Aleksander; Andersen, Rosa Linn; Brech, Andreas & Holland, Petter [Show all 9 contributors for this article] (2024). BEACH domain proteins function as cargo-sorting adaptors in secretory and endocytic pathways. Journal of Cell Biology. ISSN 0021-9525. 223(12). doi: 10.1083/jcb.202408173. Full text in Research Archive Show summary

  We identify BEACH domain–containing proteins (BDCPs) as novel membrane coat proteins involved in the sorting of transmembrane proteins (TMPs) on the trans-Golgi network and tubular sorting endosomes. The seven typical mammalian BDCPs share a predicted alpha-solenoid-beta propeller structure, suggesting they have a protocoatomer origin and function. We map the subcellular localization of seven BDCPs based on their dynamic colocalization with RAB and ARF small GTPases and identify five typical BDCPs on subdomains of dynamic tubular-vesicular compartments on the intersection of endocytic recycling and post-Golgi secretory pathways. We demonstrate that BDCPs interact directly with the cytosolic tails of selected TMPs and identify a subset of TMPs, whose trafficking to the plasma membrane is affected in cells lacking BDCP. We propose that the competitive binding of BDCPs and clathrin coat adaptors to the cytosolic tails of TMPs, followed by their clustering to distinct subdomains of secretory/recycling tubules function as a mechanism for sorting of TMPs in pleomorphic tubular-vesicular compartments that lack a clathrin coat.

• Søreng, Kristiane; Pankiv, Serhiy; Bergsmark, Camilla; Haugsten, Ellen Margrethe; Dahl, Anette Kathinka & Ballina, Laura R de la [Show all 9 contributors for this article] (2022). ALFY localizes to early endosomes and cellular protrusions to facilitate directional cell migration. Journal of Cell Science. ISSN 0021-9533. 135(4). doi: 10.1242/jcs.259138. Full text in Research Archive Show summary

  ABSTRACT Cell migration is a complex process underlying physiological and pathological processes such as brain development and cancer metastasis. The autophagy-linked FYVE protein (ALFY; also known as WDFY3), an autophagy adaptor protein known to promote clearance of protein aggregates, has been implicated in brain development and neural migration during cerebral cortical neurogenesis in mice. However, a specific role of ALFY in cell motility and extracellular matrix adhesion during migration has not been investigated. Here, we reveal a novel role for ALFY in the endocytic pathway and in cell migration. We show that ALFY localizes to RAB5- and EEA1-positive early endosomes in a PtdIns(3)P-dependent manner and is highly enriched in cellular protrusions at the leading and lagging edge of migrating cells. We find that cells lacking ALFY have reduced attachment and altered protein levels and glycosylation of integrins, resulting in the inability to form a proper leading edge and loss of directional cell motility.

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• Dahl, Anette Kathinka (2025). BEACH domain containing proteins; structure, function, and localization. Universitetet i Oslo. ISSN 9788234807190. Full text in Research Archive Show summary

  The family of nine human BEACH domain containing proteins (BDCPs) are linked to a myriad of genetic diseases and health complications. In this thesis, Anette Kathinka Dahl and co-workers provide new knowledge about the localization, structure and function of seven BDCP family members, with a focus on the typical members. Their data show that the BDCPs localize to distinct endomembrane compartments of the secretory and endocytic pathways in a gradient manner from the Golgi apparatus to the plasma membrane. Moreover, BDCPs localize to a diverse set of vesicles positive for a variety of Rab small GTPases. In the thesis it was shown how the N-terminal α-solenoid and concanavalin A-like domains in the typical BDCPs facilitate their membrane localization. The PH-BEACH-WD40 domain assembly was found to bind to cytosolic tails of transmembrane proteins such as CTLA4. The presence of both an α-solenoid region and a WD40 domain indicate that BDCPs function as novel coatomers involved in trafficking of transmembrane proteins, similarly to COPI, COPII, and clathrin. The structure of NBEAL2 was solved through Cryo-EM at a resolution of 6.6 Å. This model corresponded well with the predicted AlphaFold3 models, thus validating the theoretical models. Disease-associated point mutants in the N-terminal region of NBEAL2 were found to disrupt the specific protein localization, whereas the C-terminal mutants are hypothesized to affect its binding to and sorting of transmembrane cargo. In conclusion, the BDCPs were found to function as potential coatomers and play important roles in intracellular sorting and trafficking of transmembrane proteins. BDCPs are linked to several diseases and conditions, and further elucidation of the function of these proteins will be important in helping patients and increase our understanding of the complex cellular sorting and trafficking systems.

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