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Gene Review:

Arhgap31 - Rho GTPase activating protein 31

Mus musculus

Synonyms: 5830477L08Rik, AU041750, CdGAP, Cdc42 GTPase-activating protein, Cdgap, ...

Tcherkezian, J. et al., Jenna, S. et al., Lamarche-Vane, N. et al., Tcherkezian, J. et al., Wang, L. et al.

Lamarche-Vane, Hall,

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High impact information on Cdgap

Cdc42 GTPase-activating protein deficiency promotes genomic instability and premature aging-like phenotypes [1].
Extracellular signal-regulated kinase 1 interacts with and phosphorylates CdGAP at an important regulatory site [2].
A putative DEF (docking for ERK FXFP) domain located in the proline-rich region of CdGAP is required for efficient binding and phosphorylation by ERK1/2 [2].
We report here that CdGAP is highly phosphorylated in vivo on serine and threonine residues [2].
In platelet-derived growth factor-stimulated Swiss 3T3 cells, intersectin co-localizes with CdGAP and inhibits its GAP activity toward Rac1 [3].

Biological context of Cdgap

Also, the tissue distribution of CdGAP proteins appears to be different between human and mouse species [4].
CONCLUSIONS: Our results suggest that CdGAP properties are well conserved between human and mouse species, and that CdGAP may play an unexpected role in apoptosis [4].

Anatomical context of Cdgap

CdGAP does not show in vitro activity toward Rho, and it has no effect on lysophosphatidic acid-induced stress fiber formation when microinjected into fibroblasts [5].
Interestingly, we found that CdGAP proteins cause membrane blebbing in COS-7 cells [4].

Associations of Cdgap with chemical compounds

CdGAP consists of a N-terminal GAP domain, a central domain, and a C-terminal proline-rich domain [3].
Microinjection of CdGAP into serum-starved fibroblasts inhibits both platelet-derived growth factor-induced lamellipodia and bradykinin-induced filopodia mediated by Rac and Cdc42, respectively [5].

Regulatory relationships of Cdgap

Intersectin-Src homology 3 also inhibits CdGAP activity in GAP assays in vitro [3].

Other interactions of Cdgap

Here we show that through a subset of its Src homology 3 domains, the endocytic protein intersectin interacts with CdGAP [3].
We identify Thr776 as an in vivo target site of ERK1/2 and as an important regulatory site of CdGAP activity [2].
Furthermore, CdGAP interacts with and is phosphorylated by ERK-1 and RSK-1 in vitro [2].

References

Cdc42 GTPase-activating protein deficiency promotes genomic instability and premature aging-like phenotypes. Wang, L., Yang, L., Debidda, M., Witte, D., Zheng, Y. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
Extracellular signal-regulated kinase 1 interacts with and phosphorylates CdGAP at an important regulatory site. Tcherkezian, J., Danek, E.I., Jenna, S., Triki, I., Lamarche-Vane, N. Mol. Cell. Biol. (2005) [Pubmed]
The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin. Jenna, S., Hussain, N.K., Danek, E.I., Triki, I., Wasiak, S., McPherson, P.S., Lamarche-Vane, N. J. Biol. Chem. (2002) [Pubmed]
The human orthologue of CdGAP is a phosphoprotein and a GTPase-activating protein for Cdc42 and Rac1 but not RhoA. Tcherkezian, J., Triki, I., Stenne, R., Danek, E.I., Lamarche-Vane, N. Biol. Cell (2006) [Pubmed]
CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and Rac. Lamarche-Vane, N., Hall, A. J. Biol. Chem. (1998) [Pubmed]

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