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Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors

Yoshimura, Shin-ichiro, Gerondopoulos, Andreas, Linford, Andrea, Rigden, Daniel J., Barr, Francis A.·2010·Journal of Cell Biology
DOI 10.1083/jcb.201008051PMC PMC2958468
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Abstract

A key requirement for Rab function in membrane trafficking is site-specific activation by GDP-GTP exchange factors (GEFs), but the majority of the 63 human Rabs have no known GEF. We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are specific GEFs for 10 Rabs. DENND1A/1B localize to clathrin patches at the plasma membrane and activate Rab35 in an endocytic pathway trafficking Shiga toxin to the trans-Golgi network. DENND2 GEFs target to actin filaments and control Rab9-dependent trafficking of mannose-6-phosphate receptor to lysosomes. DENND4 GEFs target to a tubular membrane compartment adjacent to the Golgi, where they activate Rab10, which suggests a function in basolateral polarized sorting in epithelial cells that compliments the non-DENN GEF Sec2 acting on Rab8 in apical sorting. DENND1C, DENND3, DENND5A/5B, MTMR5/13, and MADD activate Rab13, Rab12, Rab39, Rab28, and Rab27A/27B, respectively. Together, these findings provide a basis for future studies on Rab regulation and function.

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  • The Retromer sub-domain proximity proteome included the RAB7 GAP TBC1D5, the RAB21/RAB32/RAB38 GEF VARP, and the RAB10 GEFs DENND4A and DENND4C.

    “These included known Retromer accessory proteins, the RAB7 GAP TBC1D546,77–81, the RAB21/RAB32/RAB38 GEF VARP (a.k.a. ANKRD27)47,48,82, and the RAB10 GEFs DENND4A and DENND4C83,84.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [83]

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Metadata

Authors
Yoshimura, S.-I., Gerondopoulos, A., Linford, A., Rigden, D. J., & Barr, F. A.
Affiliations
Cancer Research Centre 1 and 2
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2010-10-11
Volume
191
Issue
2
Pages
367-381
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201008051
PMC
PMC2958468
Cited by
317
References
2
Language
en

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