Abstract
Human ras-GTPase-activating protein (GAP120) SH3-domain-binding protein (G3BP) has recently been identified on the basis of its specific binding to the GAP120 SH3 binding domain. Here we report the identification of a mouse G3BP cDNA and the confirmation by three dimensional modelling of an RNA recognition motif (RRM) in the encoded protein. Mouse G3BP also contains an RGG domain, an acid-rich amino acid domain, and several SH3 domain-binding consensus sequences, indicating that mammalian G3BPs represent a new family of signal transduction proteins which connect tyrosine kinase-linked receptors to cellular RNA metabolism.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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DNA Primers / genetics
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DNA, Complementary / genetics
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GTPase-Activating Proteins
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Humans
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Mice
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Models, Molecular
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Molecular Sequence Data
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Polymerase Chain Reaction
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Protein Conformation
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Proteins / chemistry*
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Proteins / genetics
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Proteins / metabolism
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RNA / metabolism*
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism
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Ribonucleoprotein, U1 Small Nuclear / chemistry
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Ribonucleoprotein, U1 Small Nuclear / genetics
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Sequence Homology, Amino Acid
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Signal Transduction
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Species Specificity
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ras GTPase-Activating Proteins
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src Homology Domains
Substances
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DNA Primers
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DNA, Complementary
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GTPase-Activating Proteins
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Proteins
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RNA-Binding Proteins
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Ribonucleoprotein, U1 Small Nuclear
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U1A protein
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ras GTPase-Activating Proteins
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RNA