ArhGAP15, a novel human RacGAP protein with GTPase binding property 1

  title={ArhGAP15, a novel human RacGAP protein with GTPase binding property 
  author={Mui Leng Seoh and Chong Han Ng and Jeffery Yong and Louis Lim and Thomas Leung},
  journal={FEBS Letters},

RICH-1, a multifunctional RhoGAP domain-containing protein, involved in regulation of the actin filament system and membrane-trafficking.

Ectopic expression of the RhoGAP domain as well as the full-length protein interfered with platelet-derived growth factor BB-induced membrane ruffling, but not with serum-induced stress fiber formation, further emphasizing the notion that, in vivo, RICH-1 is a GAP for Cdc42 and Rac1.

ArhGAP15, a Rac-specific GTPase-activating Protein, Plays a Dual Role in Inhibiting Small GTPase Signaling*

The data suggest that ArhGAP15 plays a dual negative role in regulating small GTPase signaling, by acting at the level of the GTP enzyme itself, as well interacting with its effector, Pak kinase.

Plasma membrane localization affects the RhoGAP specificity of Pseudomonas ExoS

The importance of membrane localization in the targeting of Rho GTPases by ExoS RhoGAP is shown, with mutation of the C‐terminal polybasic region abolished the ability of dominant active Rac1 to protect HeLa cells from expression of the RHoGAP activity of ExoS‐MLD(RRD→N).

RPEL-family rhoGAPs link Rac/Cdc42 GTP loading to G-actin availability

ArhGAP12 mutants defective for G-actin binding exhibit more effective downregulation of Rac GTP loading following HGF stimulation and enhanced inhibition of Rac-dependent processes, including invadopodia formation.

Characterization of a Novel GTPase-activating Protein Associated with Focal Adhesions and the Actin Cytoskeleton*

A novel RhoGAP protein that interacts with actin stress fibers, focal adhesions, and cell-cell adherens junctions via its 185-amino acid C-terminal region is characterized and suggests that RC-GAP72 plays a role in regulating cell morphology and cytoskeletal organization.

Met-driven invasive growth involves transcriptional regulation of Arhgap12

Data show that HGF-driven invasive growth involves transcriptional regulation of a Rac1-specific GAP, a gene encoding a previously uncharacterized protein of the RhoGAP family, through a novel gene trapping strategy.

Assessment of functional characteristics of small GTPases using small molecules

The study has shown that R-Naproxen blocks activation of Rac1 small GTPase in ovarian cancer cells with implications for the inhibition of ovarian cancer cell proliferation, migration, and invasion.

RhoGAPs attenuate cell proliferation by direct interaction with p53 tetramerization domain.

ARHGAP15 in Human Breast Carcinoma: A Potent Tumor Suppressor Regulated by Androgens

Findings suggest that ARHGAP15 is an androgen-induced gene and has anti-tumorigenic roles associated with the Rac1 pathway, and is considered a potent prognostic factor in human breast carcinomas.



Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein.

The results indicate that ARHGAP9 is involved in regulating adhesion of hematopoietic cells to extracellular matrix.

Cloning and characterization of ARHGAP12, a novel human rhoGAP gene.

A Conserved Negative Regulatory Region in αPAK: Inhibition of PAK Kinases Reveals Their Morphological Roles Downstream of Cdc42 and Rac1

These results, coupled with previous observations with constitutively active PAK, demonstrate that these kinases play an important role downstream of Cdc42 and Rac1 in cytoskeletal reorganization.

Arabidopsis RopGAPs are a novel family of rho GTPase-activating proteins that require the Cdc42/Rac-interactive binding motif for rop-specific GTPase stimulation.

It is proposed that the CRIB domain facilitates the formation of or enhanced GAP-mediated stabilization of the transitional state of the Rop GTPase.

Residues in Cdc42 that specify binding to individual CRIB effector proteins.

Residues outside the effector loop were found to be important for binding of Cdc42 to CRIB containing proteins and also to contribute to selectivity, and should aid investigations of the role of specific effectors in CDC42 signaling in vivo.

The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia

Results suggest that n-chimaerin acts synergistically with Rac1 and Cdc42Hs to induce actin-based morphological changes and that GAPs may have morphological functions in addition to downregulation of GTPases.