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Rab10 GTPase regulates ER dynamics and morphology

English, Amber R., Voeltz, Gia K.·2013·Nature Cell Biology
DOI 10.1038/ncb2647PMC PMC3582403
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  • RAB10 has been localized to multiple subcellular compartments in different cell types including the endoplasmic reticulum, trans Golgi network, early endosomes, recycling endosomes, phagosomes, and primary cilia.

    “Consistent with this wide range of functions, RAB10 has been localized to multiple subcellular compartments in different cell types including the endoplasmic reticulum, trans Golgi network, early endosomes, recycling endosomes, phagosomes, and primary cilia (25, 31, 32, 50, 51, 52).”

    From The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes (2022) · cites this paper as [25]

    In Results, ‘Rab10 localizes to the ER’ (page not provided), the paper reports Rab10 at the ER and Golgi, but does not specify the trans-Golgi network. It reports no localization to early or recycling endosomes in the Cos-7 cells tested, and does not address phagosomes or primary cilia. Because the claim spans different cell types, the Cos-7 result does not rule out localization elsewhere. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Rab10 localizes at ER membranes and plays a role in ER dynamics and maintaining morphology.

    “Rab10 has been shown to localize at ER membranes and play a role in ER dynamics and maintaining morphology [17].”

    From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [17]

  • In neurons, RAB10 is involved in axonogenesis through the regulation of vesicular membrane trafficking toward the axonal plasma membrane.

    “In neurons, RAB10 is involved in axonogenesis through the regulation of vesicular membrane trafficking toward the axonal plasma membrane [60].”

    From Linkage, whole genome sequence, and biological data implicate variants in RAB10 in Alzheimer’s disease resilience (2017) · cites this paper as [60]

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Research works printed but not linked: 36

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  2. Terasaki, M., Chen, L. B. & Fujiwara, K. Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103, 1557–1568 (1986). · DOI
  3. Waterman-Storer, C. M. & Salmon, E. D. Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms. Curr. Biol. 8, 798–806 (1998). · DOI
  4. English, A. R., Zurek, N. & Voeltz, G. K. Peripheral ER structure and function. Curr. Opin. Cell Biol. 21, 596–602 (2009). · DOI
  5. Hu, J. et al. A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell 138, 549–561 (2009). · DOI
  6. Orso, G. et al. Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 460, 978–983 (2009). · DOI
  7. Rismanchi, N., Soderblom, C., Stadler, J., Zhu, P. P. & Blackstone, C. Atlastin GTPases are required for Golgi apparatus and ER morphogenesis. Hum. Mol. Genet. 17, 1591–1604 (2008). · DOI
  8. Murray, J. T., Panaretou, C., Stenmark, H., Miaczynska, M. & Backer, J. M. Role of Rab5 in the recruitment of hVps34/p150 to the early endosome. Traffic 3, 416–427 (2002). · DOI · Paper page
  9. Behnia, R. & Munro, S. Organelle identity and the signposts for membrane traffic. Nature 438, 597–604 (2005). · DOI
  10. Pfeffer, S. R. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11, 487–491 (2001). · DOI
  11. Cai, H., Reinisch, K. & Ferro-Novick, S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671–682 (2007). · DOI
  12. Schwartz, S. L., Cao, C., Pylypenko, O., Rak, A. & Wandinger-Ness, A. Rab GTPases at a glance. J. Cell Sci. 120, 3905–3910 (2007). · DOI
  13. Turner, M. D., Plutner, H. & Balch, W.E. A Rab GTPase is required forhomotypic assembly of the endoplasmic reticulum. J. Biol. Chem. 272, 13479–13483 (1997). · DOI
  14. Audhya, A., Desai, A. & Oegema, K. A role for Rab5 in structuring the endoplasmic reticulum. J. Cell Biol. 178, 43–56 (2007). · DOI
  15. Dreier, L. & Rapoport, T. A. In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction. J. Cell Biol. 148, 883–898 (2000). · DOI
  16. Voeltz, G. K., Prinz, W. A., Shibata, Y., Rist, J. M. & Rapoport, T. A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573–586 (2006). · DOI
  17. Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J. & van Deurs, B. Rab7: a key to lysosome biogenesis. Mol. Biol. Cell 11, 467–480 (2000). · DOI
  18. Bucci, C. et al. Co-operative regulation of endocytosis by three Rab5 isoforms. FEBS Lett. 366, 65–71 (1995). · DOI
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Metadata

Authors
English, A. R., & Voeltz, G. K.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2012-12-23
Volume
15
Issue
2
Pages
169-178
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/ncb2647
PMC
PMC3582403
Cited by
224
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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