RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo
@article{Katoh2003RhoGAR, title={RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo}, author={Hironori Katoh and Manabu Negishi}, journal={Nature}, year={2003}, volume={424}, pages={461-464} }
The small GTPase Rac has a central role in regulating the actin cytoskeleton during cell migration and axon guidance. Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs 2–4). Dock180 does not contain a conventional catalytic domain for guanine nucleotide exchange on Rac, but possesses a domain that directly binds to and specifically activates Rac1 (refs 5, 6). The small GTPase RhoG mediates several cellular morphological…
343 Citations
The DOCK180/Elmo Complex Couples ARNO-Mediated Arf6 Activation to the Downstream Activation of Rac1
- BiologyCurrent Biology
- 2005
Dock4 is regulated by RhoG and promotes Rac-dependent cell migration.
- BiologyExperimental cell research
- 2006
Exploring Rac GTPase regulation : the molecular mechanisms governing the DOCK180 and ELMO interaction and the role of this complex in Rac-mediated cell migration
- Biology
- 2011
It is concluded that, at basal levels, ELMO/DOCK180 is complexed, with ELMO in an autoinhibited state in the cytosol, and proposed that the activation state of ELMO proteins is regulated, much like in Dia-family formins, via interaction with other proteins.
Activation of Rac1 by RhoG regulates cell migration
- BiologyJournal of Cell Science
- 2006
RNA interference-mediated knockdown of RhoG in HeLa cells reduced cell migration in Transwell and scratch-wound migration assays and suggests that Rho G contributes to the regulation of Rac activity in migrating cells.
The Arf Family GTPase Arl4A Complexes with ELMO Proteins to Promote Actin Cytoskeleton Remodeling and Reveals a Versatile Ras-binding Domain in the ELMO Proteins Family*
- BiologyThe Journal of Biological Chemistry
- 2011
The present study identifies novel ELMO-interacting proteins to further define the molecular events capable of controlling ELMO recruitment to the membrane and concludes that ELMO contains a versatile RBD.
P-Rex1 directly activates RhoG to regulate GPCR-driven Rac signalling and actin polarity in neutrophils
- BiologyJournal of Cell Science
- 2014
It is shown that P-Rex1 also acts as a GEF for the Rac-related GTPase RhoG, both in vitro and in GPCR-stimulated primary mouse neutrophils, revealing a new signalling hierarchy in which P- Rex1 regulates Rac-dependent functions indirectly through RHoG-dependent recruitment of DOCK2.
ELMO 1 Directly Interacts with G βγ Subunit to Transduce GPCR Signaling to Rac 1 Activation in Chemotaxis
- Biology
- 2016
The results suggest that chemokine GPCR-mediated interaction between Gβγ and ELMO1/Dock1 complex might serve as an evolutionarily conserved mechanism for Rac activation to regulate actin cytoskeleton for chemotaxis of human cells.
Dock3 induces axonal outgrowth by stimulating membrane recruitment of the WAVE complex
- BiologyProceedings of the National Academy of Sciences
- 2010
This work identifies key conserved amino acids in the DHR-2 domain that are critical for the catalytic activity of Dock-GEFs (Dock1–4) and highlights a unique mechanism through which Dock- GEFs achieve spatial and temporal restriction of WAVE signaling.
Opening up on ELMO regulation
- BiologySmall GTPases
- 2011
It is proposed that the closed ELMO molecule masks protein-protein interfaces or domains with novel uncharacterized function; cell stimulation and GTPase binding to ELMO is proposed to activate (open) the protein and/or target the ELMO/DOCK180 complex to the cell membrane.
Endogenous RhoG is dispensable for integrin-mediated cell spreading but contributes to Rac-independent migration
- BiologyJournal of Cell Science
- 2008
It is found that constitutively active RhoG induced membrane ruffling via both Rac-dependent and -independent pathways and was important for Rac-independent cell migration, but did not significantly contribute to cell spreading even in these cells.
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