Cell. 1992 May 1;69(3):539-49.

Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from ras to the nucleus.

Settleman J, Narasimhan V, Foster LC, Weinberg RA.

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Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.

Abstract

In mitogenically stimulated and tyrosine kinase-transformed cells, a substantial fraction of the ras GTPase-activating protein (GAP) forms a complex with a protein termed p190. We have cloned several cDNAs encoding the p190 protein. Analysis of the predicted protein sequence reveals three distinct domains with homology to previously described sequences. An N-terminal domain of p190 contains sequence motifs that are found in all of the known GTPases. At the C-terminus of the protein is a domain that contains sequences very similar to those found in the breakpoint cluster region gene product, n-chimerin, and rho GAP, all of which have been shown to possess intrinsic GAP activity on small GTPases. Finally, a 778 aa segment in the middle of p190 is nearly identical in sequence to a recently described transcriptional repressor. This raises the possibility that p190, acting via GAP, can transduce signals from p21ras to the nucleus, perhaps affecting expression of specific cellular genes.

PMID:: 1581965; [PubMed - indexed for MEDLINE]

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