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J. Biol. Chem., Vol. 269, Issue 26, 17363-17366, 07, 1994
OM Rivero-Lezcano, JH Sameshima, A Marcilla and KC Robbins
To investigate the nature of proteins recognized by Src homology 3 (SH3)
domains, a cDNA expression library was prepared from macrophages and
screened with a probe representing the three SH3 domains of p47nck. Two
clones were isolated, and one, designated SAKAP I (for Src A box
Nck-associated protein I), contained the carboxyl-terminal half of the cbl
proto-oncogene product. Studies in vitro demonstrated reactivity between
SAKAP I and SH3 domains derived from a variety of molecules. Wide
variations in this assay suggested a high degree of specificity inherent in
SAKAP I binding. Moreover, it was possible to demonstrate an in vivo
association between p47nck and p120c-cbl in HL60 cells. These findings
suggest that proteins containing SH3 elements regulate Cbl function.
Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene
Laboratory of Cellular Development and Oncology, NIDR, National Institutes of Health, Bethesda, Maryland 20892.
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G. Panchamoorthy, T. Fukazawa, S. Miyake, S. Soltoff, K. Reedquist, B. Druker, S. Shoelson, L. Cantley, and H. Band p120[IMAGE] Is a Major Substrate of Tyrosine Phosphorylation upon B Cell Antigen Receptor Stimulation and Interacts in Vivo with Fyn and Syk Tyrosine Kinases, Grb2 and Shc Adaptors, and the p85 Subunit of Phosphatidylinositol 3-Kinase J. Biol. Chem., February 9, 1996; 271(6): 3187 - 3194. [Abstract] [Full Text] [PDF]
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S. P. Soltoff and L. C. Cantley p120[IMAGE] Is a Cytosolic Adapter Protein That Associates with Phosphoinositide 3-Kinase in Response to Epidermal Growth Factor in PC12 and Other Cells J. Biol. Chem., January 5, 1996; 271(1): 563 - 567. [Abstract] [Full Text] [PDF]
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T. J. Kim, Y.-T. Kim, and S. Pillai Association of Activated Phosphatidylinositol 3-Kinase with p120[IMAGE] in Antigen Receptor-ligated B Cells J. Biol. Chem., November 27, 1995; 270(46): 27504 - 27509. [Abstract] [Full Text] [PDF]
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M. L. Galisteo, I. Dikic, A. G. Batzer, W. Y. Langdon, and J. Schlessinger Tyrosine Phosphorylation of the c-cbl Proto-oncogene Protein Product and Association with Epidermal Growth Factor (EGF) Receptor upon EGF Stimulation J. Biol. Chem., September 1, 1995; 270(35): 20242 - 20245. [Abstract] [Full Text] [PDF]
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 C. Yoon, J Lee, G. Jongeward, and P. Sternberg Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl Science, August 25, 1995; 269(5227): 1102 - 1105. [Abstract] [PDF]
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T. Fukazawa, K. A. Reedquist, T. Trub, S. Soltoff, G. Panchamoorthy, B. Druker, L. Cantley, S. E. Shoelson, and H. Band The SH3 Domain-binding T Cell Tyrosyl Phosphoprotein p120 J. Biol. Chem., August 11, 1995; 270(32): 19141 - 19150. [Abstract] [Full Text] [PDF]
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S. Tanaka, L. Neff, R. Baron, and J. B. Levy Tyrosine Phosphorylation and Translocation of the c-Cbl Protein after Activation of Tyrosine Kinase Signaling Pathways J. Biol. Chem., June 16, 1995; 270(24): 14347 - 14351. [Abstract] [Full Text] [PDF]
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H. Odai, K. Sasaki, A. Iwamatsu, Y. Hanazono, T. Tanaka, K. Mitani, Y. Yazaki, and H. Hirai The Proto-oncogene Product c-Cbl Becomes Tyrosine Phosphorylated by Stimulation with GM-CSF or Epo and Constitutively Binds to the SH3 Domain of Grb2/Ash in Human Hematopoietic Cells J. Biol. Chem., May 5, 1995; 270(18): 10800 - 10805. [Abstract] [Full Text] [PDF]
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