CDC42EP2

CDC42 effector protein (Rho GTPase binding) 2
Identifiers
Symbols	CDC42EP2 ; BORG1; CEP2
External IDs	OMIM: 606132 MGI: 1929744 HomoloGene: 4933 GeneCards: CDC42EP2 Gene
Gene ontology Molecular function • opioid peptide activity • GTPase activator activity • protein binding • GTP-Rho binding Cellular component • cytoplasm • plasma membrane • endomembrane system • microtubule cytoskeleton • membrane Biological process • actin filament organization • Rho protein signal transduction • regulation of cell shape • actin cytoskeleton organization • positive regulation of actin filament polymerization • positive regulation of pseudopodium assembly • positive regulation of protein complex assembly • positive regulation of GTPase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10435	104252
Ensembl	ENSG00000149798	ENSMUSG00000045664
UniProt	O14613	Q8JZX9
RefSeq (mRNA)	NM_006779	NM_026772
RefSeq (protein)	NP_006770	NP_081048
Location (UCSC)	Chr 11: 65.31 – 65.32 Mb	Chr 19: 5.92 – 5.92 Mb
PubMed search

Cdc42 effector protein 2 is a protein that in humans is encoded by the CDC42EP2 gene.^[1][2][3]

Function

CDC42, a small Rho GTPase, regulates the formation of F-actin-containing structures through its interaction with the downstream effector proteins. The protein encoded by this gene is a member of the Borg family of CDC42 effector proteins. Borg family proteins contain a CRIB (Cdc42/Rac interactive-binding) domain. They bind to, and negatively regulate the function of, CDC42. Coexpression of this protein with dominant negative mutant CDC42 protein in fibroblast was found to induce pseudopodia formation, which suggested a role of this protein in actin filament assembly and cell shape control.^[3]

Interactions

CDC42EP2 has been shown to interact with CDC42^[1][2] and RHOQ.^[1]

References

1. Joberty G, Perlungher RR, Macara IG (Oct 1999). "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins". Molecular and Cellular Biology 19 (10): 6585–97. PMC 84628. PMID 10490598.
2. Hirsch DS, Pirone DM, Burbelo PD (Jan 2001). "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes". The Journal of Biological Chemistry 276 (2): 875–83. doi:10.1074/jbc.M007039200. PMID 11035016.
3. "Entrez Gene: CDC42EP2 CDC42 effector protein (Rho GTPase binding) 2".

Further reading

• Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (Jul 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Research 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681. PMID 9253601.
• Burbelo PD, Snow DM, Bahou W, Spiegel S (Aug 1999). "MSE55, a Cdc42 effector protein, induces long cellular extensions in fibroblasts". Proceedings of the National Academy of Sciences of the United States of America 96 (16): 9083–8. doi:10.1073/pnas.96.16.9083. PMC 17736. PMID 10430899.
• Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, Macara IG (Oct 2001). "Borg proteins control septin organization and are negatively regulated by Cdc42". Nature Cell Biology 3 (10): 861–6. doi:10.1038/ncb1001-861. PMID 11584266.
• Xue Y, Bi F, Zhang X, Zhang S, Pan Y, Liu N, Shi Y, Yao X, Zheng Y, Fan D (Jun 2006). "Role of Rac1 and Cdc42 in hypoxia induced p53 and von Hippel-Lindau suppression and HIF1alpha activation". International Journal of Cancer. Journal International Du Cancer 118 (12): 2965–72. doi:10.1002/ijc.21763. PMID 16395716.