Ingrid Kjos

• Wenzel, Eva; Pedersen, Nina Marie; Elfmark, Liv Anker; Ling, Wang; Kjos, Ingrid & Stang, Espen [Show all 10 contributors for this article] (2024). Intercellular transfer of cancer cell invasiveness via endosome-mediated protease shedding. Nature Communications. ISSN 2041-1723. 15. doi: 10.1038/s41467-024-45558-8.
• Bjørnestad, Synne Arstad; Guadagno, Noemi Antonella; Kjos, Ingrid & Progida, Cinzia (2022). Rab33b-exocyst interaction mediates localized secretion for focal adhesion turnover and cell migration. iScience. ISSN 2589-0042. 25(5). doi: 10.1016/j.isci.2022.104250. Full text in Research Archive
• Vietri, Marina; Schultz, Sebastian; Bellanger, Aurélie Nathalie Pascale; Jones, Carl; Petersen, Louise I & Raiborg, Camilla [Show all 20 contributors for this article] (2020). Unrestrained ESCRT-III drives micronuclear catastrophe and chromosome fragmention. Nature Cell Biology. ISSN 1465-7392. 22, p. 856–867. doi: 10.1038/s41556-020-0537-5. Full text in Research Archive
• Liese, Susanne; Wenzel, Eva; Kjos, Ingrid; Rojas Molina, Rossana Virginia; Schultz, Sebastian & Brech, Andreas [Show all 9 contributors for this article] (2020). Protein crowding mediates membrane remodeling in upstream ESCRT-induced formation of intraluminal vesicles. Proceedings of the National Academy of Sciences of the United States of America. ISSN 0027-8424. 117(46), p. 28614–28624. doi: 10.1073/pnas.2014228117. Show summary

  As part of the lysosomal degradation pathway, the endosomal sorting complexes required for transport (ESCRT-0-III/VPS4) sequester receptors at the endosome and simultaneously deform the membrane to generate intraluminal vesicles (ILVs). Whereas ESCRT-III/VPS4 have an established function in ILV formation, the role of upstream ESCRTs (0-II) in membrane shape remodeling is not understood. Combining experimental measurements and electron microscopy analysis of ESCRT-III depleted cells with a mathematical model, we show that upstream ESCRT-induced alteration of the Gaussian bending rigidity and their crowding in concert with the transmembrane cargo on the membrane induces membrane deformation and facilitates ILV formation: upstream ESCRT-driven budding does not require ATP consumption as only a small energy barrier needs to be overcome. Our model predicts that ESCRTs do not become part of the ILV, but localize with a high density at the membrane neck, where the steep decline in the Gaussian curvature likely triggers ESCRT-III/VPS4 assembly to enable neck constriction and scission.

• Guadagno, Noemi Antonella; Margiotta, Azzurra; Bjørnestad, Synne Arstad; Haugen, Linda Hofstad; Kjos, Ingrid & Xiaochun, Xu [Show all 10 contributors for this article] (2020). Rab18 regulates focal adhesion dynamics by interacting with kinectin-1 at the endoplasmic reticulum . Journal of Cell Biology. ISSN 0021-9525. 219(7), p. 1–23. doi: 10.1083/JCB.201809020. Full text in Research Archive Show summary

  The members of the Rab family of small GTPases are molecular switches that regulate distinct steps in different membrane traffic pathways. In addition to this canonical function, Rabs can play a role in other processes, such as cell adhesion and motility. Here, we reveal the role of the small GTPase Rab18 as a positive regulator of directional migration in chemotaxis, and the underlying mechanism. We show that knockdown of Rab18 reduces the size of focal adhesions (FAs) and influences their dynamics. Furthermore, we found that Rab18, by directly interacting with the endoplasmic reticulum (ER)-resident protein kinectin-1, controls the anterograde kinesin-1–dependent transport of the ER required for the maturation of nascent FAs and protrusion orientation toward a chemoattractant. Altogether, our data support a model in which Rab18 regulates kinectin-1 transport toward the cell surface to form ER–FA contacts, thus promoting FA growth and cell migration during chemotaxis

• Vestre, Katharina; Kjos, Ingrid; Guadagno, Noemi Antonella; Distefano, Marita Borg; Kohler, Felix & Fenaroli, Federico [Show all 8 contributors for this article] (2019). Rab6 regulates cell migration and invasion by recruiting Cdc42 and modulating its activity. Cellular and Molecular Life Sciences (CMLS). ISSN 1420-682X. 76(13), p. 2593–2614. doi: 10.1007/s00018-019-03057-w. Full text in Research Archive
• Distefano, Marita Borg; Haugen, Linda Hofstad; Wang, Yan; Perdreau-Dahl, Harmonie; Kjos, Ingrid & Jia, Da [Show all 10 contributors for this article] (2018). TBC1D5 controls the GTPase cycle of Rab7b. Journal of Cell Science. ISSN 0021-9533. 131(17), p. 1–13. doi: 10.1242/jcs.216630. Full text in Research Archive
• Kjos, Ingrid; Vestre, Katharina; Guadagno, Noemi Antonella; Distefano, Marita Borg & Progida, Cinzia (2018). Rab and Arf proteins at the crossroad between membrane transport and cytoskeleton dynamics. BBA - Molecular Cell Research. ISSN 0167-4889. 1865(10), p. 1397–1409. doi: 10.1016/j.bbamcr.2018.07.009. Full text in Research Archive
• Kjos, Ingrid; Distefano, Marita Borg; Sætre, Frank Ove; Repnik, Urska; Holland, Petter & Jones, Arwyn T [Show all 10 contributors for this article] (2017). Rab7b modulates autophagic flux by interacting with Atg4B. EMBO Reports. ISSN 1469-221X. 18(10), p. 1727–1739. doi: 10.15252/embr.201744069. Full text in Research Archive
• Dick, Gunnar; Akslen-Hoel, Linn Kristin; Grøndahl, Frøy; Kjos, Ingrid; Maccarana, Marco & Prydz, Kristian (2015). PAPST1 regulates sulfation of heparan sulfate proteoglycans in epithelial MDCK II cells. Glycobiology. ISSN 0959-6658. 25(1), p. 30–41. doi: 10.1093/glycob/cwu084.
• Dick, Gunnar; Akslen-Hoel, Linn Kristin ; Grøndahl, Frøy; Kjos, Ingrid & Prydz, Kristian (2012). Proteoglycan Synthesis and Golgi Organization in Polarized Epithelial Cells. Journal of Histochemistry and Cytochemistry. ISSN 0022-1554. 60(12), p. 926–935. doi: 10.1369/0022155412461256. Show summary

  A large number of complex glycosylation mechanisms take place in the Golgi apparatus. In epithelial cells, glycosylated protein molecules are transported to both the apical and the basolateral surface domains. Although the prevailing view is that the Golgi apparatus provides the same lumenal environment for glycosylation of apical and basolateral cargo proteins, there are indications that proteoglycans destined for the two opposite epithelial surfaces are exposed to different conditions in transit through the Golgi apparatus. We will here review data relating proteoglycan and glycoprotein synthesis to characteristics of the apical and basolateral secretory pathways in epithelial cells.

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• Distefano, Marita Borg; Kjos, Ingrid; Bakke, Oddmund & Progida, Cinzia (2015). Rab7b at the intersection of intracellular trafficking and cell migration. Communicative & Integrative Biology. ISSN 1942-0889. 8(6). doi: 10.1080/19420889.2015.1023492.

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