Lamarche-Vane N - Search Results

1

A DLG1-ARHGAP31-CDC42 axis is essential for the intestinal stem cell response to fluctuating niche Wnt signaling.

Castillo-Azofeifa D, Wald T, Reyes EA, Gallagher A, Schanin J, Vlachos S, Lamarche-Vane N, Bomidi C, Blutt S, Estes MK, Nystul T, Klein OD. Castillo-Azofeifa D, et al. Among authors: lamarche vane n. Cell Stem Cell. 2023 Feb 2;30(2):188-206.e6. doi: 10.1016/j.stem.2022.12.008. Epub 2023 Jan 13. Cell Stem Cell. 2023. PMID: 36640764 Free PMC article.

2

CdGAP/ARHGAP31, a Cdc42/Rac1 GTPase regulator, is critical for vascular development and VEGF-mediated angiogenesis.

Caron C, DeGeer J, Fournier P, Duquette PM, Luangrath V, Ishii H, Karimzadeh F, Lamarche-Vane N, Royal I. Caron C, et al. Sci Rep. 2016 Jun 7;6:27485. doi: 10.1038/srep27485. Sci Rep. 2016. PMID: 27270835 Free PMC article.

3

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 EI, Lamarche-Vane N. Tcherkezian J, et al. Biol Cell. 2006 Aug;98(8):445-56. doi: 10.1042/BC20050101. Biol Cell. 2006. PMID: 16519628

4

Current knowledge of the large RhoGAP family of proteins.

Tcherkezian J, Lamarche-Vane N. Tcherkezian J, et al. Biol Cell. 2007 Feb;99(2):67-86. doi: 10.1042/BC20060086. Biol Cell. 2007. PMID: 17222083 Review.

5

CdGAP is required for transforming growth factor β- and Neu/ErbB-2-induced breast cancer cell motility and invasion.

He Y, Northey JJ, Primeau M, Machado RD, Trembath R, Siegel PM, Lamarche-Vane N. He Y, et al. Oncogene. 2011 Mar 3;30(9):1032-45. doi: 10.1038/onc.2010.477. Epub 2010 Nov 1. Oncogene. 2011. PMID: 21042277

6

Cdc42 GTPase-activating protein (CdGAP) interacts with the SH3D domain of Intersectin through a novel basic-rich motif.

Primeau M, Ben Djoudi Ouadda A, Lamarche-Vane N. Primeau M, et al. FEBS Lett. 2011 Mar 23;585(6):847-53. doi: 10.1016/j.febslet.2011.02.022. Epub 2011 Feb 22. FEBS Lett. 2011. PMID: 21349274 Free article.

7

Gain-of-function mutations of ARHGAP31, a Cdc42/Rac1 GTPase regulator, cause syndromic cutis aplasia and limb anomalies.

Southgate L, Machado RD, Snape KM, Primeau M, Dafou D, Ruddy DM, Branney PA, Fisher M, Lee GJ, Simpson MA, He Y, Bradshaw TY, Blaumeiser B, Winship WS, Reardon W, Maher ER, FitzPatrick DR, Wuyts W, Zenker M, Lamarche-Vane N, Trembath RC. Southgate L, et al. Am J Hum Genet. 2011 May 13;88(5):574-85. doi: 10.1016/j.ajhg.2011.04.013. Am J Hum Genet. 2011. PMID: 21565291 Free PMC article.

8

A stretch of polybasic residues mediates Cdc42 GTPase-activating protein (CdGAP) binding to phosphatidylinositol 3,4,5-trisphosphate and regulates its GAP activity.

Karimzadeh F, Primeau M, Mountassif D, Rouiller I, Lamarche-Vane N. Karimzadeh F, et al. J Biol Chem. 2012 Jun 1;287(23):19610-21. doi: 10.1074/jbc.M112.344606. Epub 2012 Apr 19. J Biol Chem. 2012. PMID: 22518840 Free PMC article.

9

CdGAP is a talin-binding protein and a target of TGF-β signaling that promotes HER2-positive breast cancer growth and metastasis.

He Y, Goyette MA, Chapelle J, Boufaied N, Al Rahbani J, Schonewolff M, Danek EI, Muller WJ, Labbé DP, Côté JF, Lamarche-Vane N. He Y, et al. Among authors: lamarche vane n. Cell Rep. 2023 Aug 29;42(8):112936. doi: 10.1016/j.celrep.2023.112936. Epub 2023 Aug 7. Cell Rep. 2023. PMID: 37552602 Free article.

10

The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin.

Jenna S, Hussain NK, Danek EI, Triki I, Wasiak S, McPherson PS, Lamarche-Vane N. Jenna S, et al. J Biol Chem. 2002 Feb 22;277(8):6366-73. doi: 10.1074/jbc.M105516200. Epub 2001 Dec 13. J Biol Chem. 2002. PMID: 11744688 Free article.

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