Cloning and characterization of proteins that bind the sh3 domains of the nck adaptor protein

Lawrence Quilliam, J. K. Westwick, C. J. Der, Q. T. Lambert

Research output: Contribution to journalArticle

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Abstract

Nck is a SH2- and SH3-containing adaptor molecule that associates with activated receptor protein tyrosine kinases (PTKs). Bacterial expression libraries were screened to identify Nck SH3-binding proteins that might serve as PTK effectors. One cDNA isolated encoded the Wiskott-Aldrich syndrome protein (WASP), responsible for an inheritable immunodeficiency disease. WASP contained multiple putative SH3-binding motifs and was found to bind to the Nck, Src, PLase C and Grb2 SH3 domains in vitro. A second Nck-binding clone encoded PRK2 a PKC-related ser/thr kinase. PRK2 interacted specifically with the 2nd SH3 domain of Nck vs. those of Src, Abl, Grb2, Crk, p120 GAP or NADPH oxidase p67. Overexpression of Nck or PRK2 induced unique morphological changes in NIH3T3 cells. Data will be presented on the role of Nck and PRK2 in cytoskeletal regulation and transcriptional activation.

Original languageEnglish
JournalFASEB Journal
Volume10
Issue number6
StatePublished - 1996

Fingerprint

Wiskott-Aldrich Syndrome Protein
src Homology Domains
Cloning
p120 GTPase Activating Protein
Organism Cloning
molecular cloning
receptor protein-tyrosine kinase
protein-tyrosine kinases
NADPH Oxidase
immunosuppression
Receptor Protein-Tyrosine Kinases
transcriptional activation
Protein-Tyrosine Kinases
Transcriptional Activation
binding proteins
Carrier Proteins
phosphotransferases (kinases)
Proteins
Phosphotransferases
proteins

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Cloning and characterization of proteins that bind the sh3 domains of the nck adaptor protein. / Quilliam, Lawrence; Westwick, J. K.; Der, C. J.; Lambert, Q. T.

In: FASEB Journal, Vol. 10, No. 6, 1996.

Research output: Contribution to journalArticle

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