Rab35, acting through ACAP2 switching off Arf6, negatively regulates oligodendrocyte differentiation and myelination

Miyamoto, Yuki; Yamamori, Natsuki; Torii, Tomohiro; Tanoue, Akito; Yamauchi, Junji

doi:10.1091/mbc.e13-10-0600

Cited by 41 publications

(48 citation statements)

References 60 publications

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“…Altogether, there is clear evidence that Rab35 negatively regulates ARF6 activation on recycling endosomes, which is important for correct recycling of cargoes. Such a Rab35/ARF6 antagonism has been further confirmed during the regulation of oligodendrocyte differentiation (46).…”

Section: Mical-l1 and Acap2mentioning

confidence: 75%

Rab35 GTPase: A Central Regulator of Phosphoinositides and F‐actin in Endocytic Recycling and Beyond

Klinkert

Échard

2016

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Rab35 is one of the first discovered members of the large Rab GTPase family, yet it received little attention for 10 years being considered merely as a Rab1-like GTPase. In 2006, Rab35 was recognized as a unique Rab GTPase localized both at the plasma membrane and on endosomes, playing essential roles in endocytic recycling and cytokinesis. Since then, Rab35 has become one of the most studied Rabs involved in a growing number of cellular functions, including endosomal trafficking, exosome release, phagocytosis, cell migration, immunological synapse formation and neurite outgrowth. Recently, Rab35 has been acknowledged as an oncogenic GTPase with activating mutations being found in cancer patients. In this review, we provide a comprehensive summary of known Rab35-dependent cellular functions and detail the few Rab35 effectors characterized so far. We also review how the Rab35 GTP/GDP cycle is regulated, and emphasize a newly discovered mechanism that controls its tight activation on newborn endosomes. We propose that the involvement of Rab35 in such diverse and apparently unrelated cellular functions can be explained by the central role of this GTPase in regulating phosphoinositides and F-actin, both on endosomes and at the plasma membrane.

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Section: Mical-l1 and Acap2mentioning

confidence: 75%

Rab35 GTPase: A Central Regulator of Phosphoinositides and F‐actin in Endocytic Recycling and Beyond

Klinkert

Échard

2016

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“…Rab35 is one such Rab protein and has been shown to bind various candidate effector molecules, including MICAL-1 (7), MICAL-L1 (7,9,10), MICAL-cl (7), OCRL (7,11), RUSC2 (12), Fascin1 (13), and centaurin-␤2 (8,14), and to be involved in various cellular events, including cytokinesis (11,15,16), cell migration (17,18), phagocytosis (19,20), immunological synapse formation (21), myelination (22), and neurite outgrowth (10,14,23,24), most likely through regulation of endocytic recycling (25). The pleiotropic roles of Rab35 in membrane trafficking may be attributable to the presence of multiple Rab35 effectors, but the involvement of individual Rab35 effectors in the above cellular events has remained largely unknown.…”

mentioning

confidence: 99%

Structure-Function Analyses of the Small GTPase Rab35 and Its Effector Protein Centaurin-β2/ACAP2 during Neurite Outgrowth of PC12 Cells

Etoh

Fukuda

2015

Journal of Biological Chemistry

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Background: Centaurin-␤2 specifically recognizes Rab35 but not the other 59 Rabs. Results: The T76S/T81A mutation in the switch II region of Rab35 specifically impaired its centaurin-␤2 binding activity. Conclusion: Thr-76 and Thr-81 are key residues of Rab35 for the specific recognition by centaurin-␤2. Significance: Rab35(T76S/T81A) should be a useful tool for evaluating the functional significance of the Rab35/centaurin-␤2 interaction in Rab35-dependent cellular events.

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“…Our studies uncover a protein network promoting linker cell engulfment and degradation ( Figure 7A). We find [42][43][44][45][46] . In some of these cases, interactions between RAB-35 and putative ARF-6 GAPs are seen 47 .…”

Section: Inactivation Of Apoptosis Genes Also Only Weakly Interferesmentioning

confidence: 82%

RAB-35 and ARF-6 GTPases Mediate Engulfment and Clearance Following Linker Cell-Type Death

Kutscher

Keil

Shaham

2017

Preprint

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Clearance of dying cells is essential for development and homeostasis. Conserved genes mediate apoptotic cell removal, but whether these genes also control non-apoptotic cell removal is a major open question. Linker cell-type death (LCD) is a prevalent non-apoptotic developmental cell death process with features conserved from C. elegans to vertebrates. Using microfluidics-based long-term in vivo imaging, we show that unlike apoptotic cells, the C. elegans linker cell, which dies by LCD, is competitively phagocytosed by two neighboring cells, resulting in cell splitting. Subsequent cell elimination does not require apoptotic engulfment genes. Rather, we find that RAB-35 GTPase is a key coordinator of competitive phagocytosis onset and linker cell degradation. RAB-35 binds CNT-1, an ARF-6 GTPase activating protein; removes ARF-6, a degradation inhibitor, from phagosome membranes; and recruits RAB-5 and RAB-7 GTPases for phagolysosome maturation. We propose that RAB-35 and ARF-6 drive an evolutionarily conserved program eliminating cells dying by LCD.

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Rab35, acting through ACAP2 switching off Arf6, negatively regulates oligodendrocyte differentiation and myelination

Cited by 41 publications

References 60 publications

Rab35 GTPase: A Central Regulator of Phosphoinositides and F‐actin in Endocytic Recycling and Beyond

Rab35 GTPase: A Central Regulator of Phosphoinositides and F‐actin in Endocytic Recycling and Beyond

Structure-Function Analyses of the Small GTPase Rab35 and Its Effector Protein Centaurin-β2/ACAP2 during Neurite Outgrowth of PC12 Cells

RAB-35 and ARF-6 GTPases Mediate Engulfment and Clearance Following Linker Cell-Type Death

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