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Rab35: GEFs, GAPs and Effectors
Abstract
Rabs are the largest family of small GTPases and are master regulators of membrane trafficking. Following activation by guanine‐nucleotide exchange factors (GEFs), each Rab binds a specific set of effector proteins that mediate the various downstream functions of that Rab. Then, with the help of GTPase‐activating proteins, the Rab converts GTP to GDP, terminating its function. There are over 60 Rabs in humans and only a subset has been analyzed in any detail. Recently, Rab35 has emerged as a key regulator of cargo recycling at endosomes, with an additional role in regulation of the actin cytoskeleton. Here, we will focus on the regulation of Rab35 activity by the connecdenn/DENND1 family of GEFs and the TBC1D10/EPI64 family of GTPase‐activating proteins. We will describe how analysis of these proteins, as well as a plethora of Rab35 effectors has provided insights into Rab35 function. Finally, we will describe how Rab35 provides a novel link between the Rab and Arf family of GTPases with implications for tumor formation and invasiveness.
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Rab35 is essential for inactivation of ARF6.
“Rab35 is essential for inactivation of ARF6 (Chaineau et al., 2013).”
From ApoE4 Alters ABCA1 Membrane Trafficking in Astrocytes (2019) · cites this paper as Chaineau et al., 2013
The ACAP2 section says Rab35 recruits ACAP2, whose GAP activity inactivates Arf6. The ‘Relationship between Rab35 and Arf6’ section describes this inhibition in specific cellular processes, but does not establish that Rab35 is essential for Arf6 inactivation generally. (LLM, conf=0.85)
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Cites
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RETRACTED ARTICLE: LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Bae, E.-J., Kim, D.-K., Kim, C., Mante, M., Adame, A., Rockenstein, E., Ulusoy, A., Klinkenberg, M., Jeong, G. R., Bae, J. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05958-z · Cited by 149
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Fischer, B., Lüthy, K., Paesmans, J., De Koninck, C., Maes, I., Swerts, J., Kuenen, S., Uytterhoeven, V., Verstreken, P., & Versées, W. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3297 · Cited by 62
Metadata
- Authors
- Chaineau, M., Ioannou, M. S., & McPherson, P. S.
- Affiliations
- Department of Neurology and Neurosurgery, Montreal Neurological Institute McGill University Montreal Quebec H3A 2B4 Canada
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2013-08-21
- Volume
- 14
- Issue
- 11
- Pages
- 1109-1117
- ISSN
- 1398-9219
- 1600-0854
- Cited by
- 114
- References
- 3
- Language
- en
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