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Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins

Name: Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins
Creator: Ponting, Chris P.
Keywords: 0301 basic medicine, 0303 health sciences, Sequence Homology, Amino Acid, GTPase-Activating Proteins, Molecular Sequence Data, Animal Population Groups, Protein Structure, Tertiary, Proto-Oncogene Proteins c-raf, 03 medical and health sciences, Species Specificity

descriptionPublicationkeyboard_double_arrow_right Article 01 Oct 1999 English Publisher:Springer Science and Business Media LLCJournal:Journal of Molecular Medicine, volume 77, pages 695-698 (issn: 0946-2716, eissn: 1432-1440,

Authors: Ponting, Chris P.;

doi: 10.1007/s001099900054

pmid: 10606204

Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins

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Abstract

Ras proteins play critical roles in regulating cell growth and differentiation, and mutated Ras genes are expressed in a variety of human cancers. Consequently, much interest has centered on the binding partners of Ras, including the Ras-binding domain (RBD) of Raf kinase. Here evidence is presented that domains homologous to the Raf RBD are present in tandem in RGS12, RGS14 and LOCO, and singly in molecules similar to mouse Tiam-1. In addition, RGS12, RGS14 and LOCO are shown to contain single "LGN motifs" that are guanine nucleotide exchange factors specific for the alpha-subunit of G proteins. These findings indicate "cross-talk" interactions between signalling pathways involving Ras and Rap and pathways involving Rho, Rac and G alpha GTPases.

Related Organizations

National Institute of Health
Pakistan
National Center for Biotechnology Information
United States
National Institutes of Health
United States
United States National Library of Medicine
United States

Keywords

Sequence Homology, Amino Acid, GTPase-Activating Proteins, Molecular Sequence Data, Animal Population Groups, Protein Structure, Tertiary, Proto-Oncogene Proteins c-raf, Species Specificity, Consensus Sequence, ras Proteins, Animals, Humans, Amino Acid Sequence, Sequence Alignment, RGS Proteins, Protein Binding, Signal Transduction

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