Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains.
In the second of a series of experiments designed to identify p47nck-Src homology 3 (SH3)-binding molecules, we report the cloning of SAKAP II (Src A box Nck-associated protein II) from an HL60 cDNA expression library. This molecule has been identified as a cDNA encoding the protein product of WASP, which ... is mutated in Wiskott-Aldrich syndrome patients. Studies in vivo and in vitro demonstrated a highly specific interaction between the SH3 domains of p47nck and Wiskott-Aldrich syndrome protein. Furthermore, anti-Wiskott-Aldrich syndrome protein antibodies recognized a protein of 66 kDa by Western blot (immunoblot) analysis. In vitro translation studies identified the 66-kDa protein as the protein product of WASP, and subcellular fractionation experiments showed that p66WASP is mainly present in the cytosol fraction, although significant amounts are also present in membrane and nuclear fractions. The main p47nck region implicated in the association with p66WASP was found to be the carboxy-terminal SH3 domain.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Antibodies, Cell Membrane, Cell Nucleus, Cloning, Molecular, Cytosol, Genes, Humans, Oncogene Proteins, Protein Biosynthesis, Proteins, Sequence Analysis, DNA, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Wiskott-Aldrich Syndrome, Wiskott-Aldrich Syndrome Protein
Adaptor Proteins, Signal Transducing, Antibodies, Cell Membrane, Cell Nucleus, Cloning, Molecular, Cytosol, Genes, Humans, Oncogene Proteins, Protein Biosynthesis, Proteins, Sequence Analysis, DNA, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Wiskott-Aldrich Syndrome, Wiskott-Aldrich Syndrome Protein
Mol. Cell. Biol.
Date: Oct. 01, 1995
PubMed ID: 7565724
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