Literature DB >> 9838117

Cloning, genomic organization and chromosomal assignment of the mouse p190-B gene.

P D Burbelo1, A A Finegold, C A Kozak, Y Yamada, H Takami.   

Abstract

The p190 family of GTPases consists of at least two different isoforms both containing an N-terminal GTPase and a C-terminal Rho GAP domain. Here we have isolated and characterized genomic and cDNA clones spanning the entire coding region of the mouse p190-B gene. Genomic data were obtained by sequencing plasmid subclones of two overlapping mouse genomic phage clones. Interestingly, a single 3.9 kb exon was found to contain approx. 80% of the coding region of the mouse p190-B protein (amino acid residues 1-1238) including the 5'-untranslated region, the N-terminal GTPase domain and a middle domain of unknown function. Missing from this exon, however, was the C-terminal Rho GAP domain, which was cloned from mouse brain mRNA using reverse transcriptase polymerase chain reaction. Comparison of the mouse with the human p190-B proteins revealed that approx. 97% of the amino acid residues were identical. Northern analysis of total RNA from a variety of mouse tissues detected ubiquitous expression of two p190-B transcripts of 4.0 and 6.8 kb in size. Analysis of two multilocus genetic crosses localized the mouse gene, Gfi2, to a position on chromosome 12, consistent with the mapping of the human gene to a position of conserved synteny on chromosome 14. The high level of sequence homology between the human and the mouse suggests that there is a strong selective pressure to maintain the p190-B protein structure.

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Year:  1998        PMID: 9838117     DOI: 10.1016/s0167-4781(98)00207-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

Review 1.  Regulation of Rho GTPase activity at the leading edge of migrating cells by p190RhoGAP.

Authors:  Aurélien Bidaud-Meynard; Fabien Binamé; Valérie Lagrée; Violaine Moreau
Journal:  Small GTPases       Date:  2017-03-13

2.  Extracellular signal-regulated kinase promotes Rho-dependent focal adhesion formation by suppressing p190A RhoGAP.

Authors:  Ashok K Pullikuth; Andrew D Catling
Journal:  Mol Cell Biol       Date:  2010-05-03       Impact factor: 4.272

Review 3.  Interplay between FAK, PKCδ, and p190RhoGAP in the regulation of endothelial barrier function.

Authors:  Katie L Grinnell; Elizabeth O Harrington
Journal:  Microvasc Res       Date:  2011-04-22       Impact factor: 3.514

4.  Neutrophil functions and autoimmune arthritis in the absence of p190RhoGAP: generation and analysis of a novel null mutation in mice.

Authors:  Tamás Németh; Krisztina Futosi; Csilla Hably; Madeleine R Brouns; Sascha M Jakob; Miklós Kovács; Zsuzsanna Kertész; Barbara Walzog; Jeffrey Settleman; Attila Mócsai
Journal:  J Immunol       Date:  2010-07-30       Impact factor: 5.422

Review 5.  p190RhoGAPs, the ARHGAP35- and ARHGAP5-Encoded Proteins, in Health and Disease.

Authors:  Capucine Héraud; Mathilde Pinault; Valérie Lagrée; Violaine Moreau
Journal:  Cells       Date:  2019-04-12       Impact factor: 6.600

6.  RhoA is down-regulated at cell-cell contacts via p190RhoGAP-B in response to tensional homeostasis.

Authors:  Suzanne M Ponik; Steven M Trier; Michele A Wozniak; Kevin W Eliceiri; Patricia J Keely
Journal:  Mol Biol Cell       Date:  2013-04-03       Impact factor: 4.138

  6 in total

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