The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Rab10 is involved in basolateral transport in polarized Madin-Darby canine kidney cells
Abstract
The sorting of newly synthesized membrane proteins to the cell surface is an important mechanism of cell polarity. To identify more of the molecular machinery involved, we investigated the function of the small GTPase Rab10 in polarized epithelial Madin–Darby canine kidney cells. We find that GFP‐tagged Rab10 localizes primarily to the Golgi during early cell polarization. Expression of an activated Rab10 mutant inhibits biosynthetic transport from the Golgi and missorts basolateral cargo to the apical membrane. Depletion of Rab10 by RNA interference has only mild effects on biosynthetic transport and epithelial polarization, but simultaneous inhibition of Rab10 and Rab8a more strongly impairs basolateral sorting. These results indicate that Rab10 functions in trafficking from the Golgi at early stages of epithelial polarization, is involved in biosynthetic transport to the basolateral membrane and may co‐operate with Rab8.
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GDP-locked T23N RAB10 has significantly decreased steady-state protein levels compared to wild-type RAB10.
“we observed significantly decreased steady-state protein levels for the GDP-locked mutant by both immunoblotting (Fig. 3D) and immunofluorescence (Fig. 3E).”
From The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes (2022) · cites this paper as [34]
Rab10 is involved in recycling and present at the trans-Golgi network (TGN).
“In addition, previously it has been shown that Rab10 is involved recycling and present at the trans-Golgi network (TGN) [12, 72].”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [72]
RAB10 modulates a variety of membrane trafficking events including exocytic polarized targeting and endocytic recycling, and can perform functions partially redundant with RAB8A.
“RAB10 has been described to modulate a variety of membrane trafficking events including exocytic polarized targeting and endocytic recycling events [41], and can perform functions partially redundant with those of RAB8A [42,43,44,45].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [43]
RAB8 and RAB10 can cooperatively regulate other vesicular trafficking pathways including basolateral sorting, neurite outgrowth, and ciliogenesis.
“and with previous reports showing that RAB8 and RAB10 can cooperatively regulate other vesicular trafficking pathways including basolateral sorting, neurite outgrowth, and ciliogenesis [42,43,44,45].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [43]
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Sorted by citations
A Role for Autophagy in the Extension of Lifespan by Dietary Restriction in C. elegans
Hansen, M., Chandra, A., Mitic, L. L., Onken, B., Driscoll, M., & Kenyon, C. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.0040024 · Cited by 766
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LRRK2 and Rab10 coordinate macropinocytosis to mediate immunological responses in phagocytes
Liu, Z., Xu, E., Zhao, H. T., Cole, T., & West, A. B. (2020) · The EMBO Journal · doi:10.15252/embj.2020104862 · Cited by 90
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Khan, T. G., Ginsburg, D., & Emmer, B. T. (2022) · Journal of Lipid Research · doi:10.1016/j.jlr.2022.100248 · Cited by 21
Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain
Singh, V., Menard, M. A., Serrano, G. E., Beach, T. G., Zhao, H. T., Riley-DiPaolo, A., Subrahmanian, N., LaVoie, M. J., & Volpicelli-Daley, L. A. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01704-9 · Cited by 9
Metadata
- Authors
- Schuck, S., Gerl, M. J., Ang, A., Manninen, A., Keller, P., Mellman, I., & Simons, K.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2006-10-18
- Volume
- 8
- Issue
- 1
- Pages
- 47-60
- ISSN
- 1398-9219
- 1600-0854
- Cited by
- 117
- References
- 1
- Language
- en
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