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Atypical Rho GTPases of the RhoBTB Subfamily: Roles in vesicle trafficking and tumorigenesis

Ji, Wei; Rivero, Francisco

Authors

Wei Ji



Abstract

RhoBTB proteins constitute a subfamily of atypical Rho GTPases represented in mammals by RhoBTB1, RhoBTB2, and RhoBTB3. Their characteristic feature is a carboxyl terminal extension that harbors two BTB domains capable of assembling cullin 3-dependent ubiquitin ligase complexes. The expression of all three RHOBTB genes has been found reduced or abolished in a variety of tumors. They are considered tumor suppressor genes and recent studies have strengthened their implication in tumorigenesis through regulation of the cell cycle and apoptosis. RhoBTB3 is also involved in retrograde transport from endosomes to the Golgi apparatus. One aspect that makes RhoBTB proteins atypical among the Rho GTPases is their proposed mechanism of activation. No specific guanine nucleotide exchange factors or GTPase activating proteins are known. Instead, RhoBTB might be activated through interaction with other proteins that relieve their auto-inhibited conformation and inactivated through auto-ubiquitination and destruction in the proteasome. In this review we discuss our current knowledge on the molecular mechanisms of action of RhoBTB proteins and the implications for tumorigenesis and other pathologic conditions.

Citation

Ji, W., & Rivero, F. (2016). Atypical Rho GTPases of the RhoBTB Subfamily: Roles in vesicle trafficking and tumorigenesis. Cells, 5(2), 28. https://doi.org/10.3390/cells5020028

Journal Article Type Review
Acceptance Date Jun 8, 2016
Online Publication Date Jun 14, 2016
Publication Date Jun 14, 2016
Deposit Date Jun 10, 2016
Publicly Available Date Mar 28, 2024
Journal Cells
Electronic ISSN 2073-4409
Publisher MDPI
Peer Reviewed Peer Reviewed
Volume 5
Issue 2
Article Number ARTN 28
Pages 28
DOI https://doi.org/10.3390/cells5020028
Keywords Cullin, Cyclin E, HIFα, Rab9, RhoBTB, Tumor suppressor, Ubiquitination
Public URL https://hull-repository.worktribe.com/output/439437
Publisher URL http://www.mdpi.com/2073-4409/5/2/28
Additional Information This is a copy of an article published in: Cells, 2016, v.5 issue 2.

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