A phosphorylation-dependent gating mechanism controls the SH2 domain interactions of the Shc adaptor protein.

[1]  S. Blacklow,et al.  The dual-function disabled-1 PTB domain exhibits site independence in binding phosphoinositide and peptide ligands. , 2004, Biochemistry.

[2]  Ming-Ming Zhou,et al.  Coupling of folding and binding in the PTB domain of the signaling protein Shc. , 2003, Structure.

[3]  Johannes Buchner,et al.  p53 contains large unstructured regions in its native state. , 2002, Journal of molecular biology.

[4]  M. N. Poy,et al.  Shc and CEACAM1 Interact to Regulate the Mitogenic Action of Insulin* , 2002, The Journal of Biological Chemistry.

[5]  G. D. Vita,et al.  The insulin receptor substrate (IRS)-1 recruits phosphatidylinositol 3-kinase to Ret: evidence for a competition between Shc and IRS-1 for the binding to Ret , 2001, Oncogene.

[6]  M. Welham,et al.  Shc associates with the IL-3 receptor β subunit, SHIP and Gab2 following IL-3 stimulation , 2000 .

[7]  R. Schmandt,et al.  Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells , 1999, Oncogene.

[8]  C. McGlade,et al.  Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc , 1998, Oncogene.

[9]  Y. Kido,et al.  Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. , 1998, Molecular endocrinology.

[10]  M. Shibuya,et al.  Tyrosine residues 239 and 240 of Shc are phosphatidylinositol 4,5-bisphosphate-dependent phosphorylation sites by c-Src. , 1997, Biochemical and biophysical research communications.

[11]  L. Frati,et al.  Selective binding of shc-SH2 domain to tyrosine-phosphorylated zeta but not gamma-chain upon CD16 ligation on human NK cells. , 1997, Journal of immunology.

[12]  J. C. Pratt,et al.  Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo , 1997, Molecular and cellular biology.

[13]  L. Cantley,et al.  A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains* , 1997, The Journal of Biological Chemistry.

[14]  F. Hayashi,et al.  Phosphatidylinositol 4,5‐bisphosphate stimulates phosphorylation of the adaptor protein Shc by c‐Src , 1997, FEBS letters.

[15]  G. Carpenter,et al.  Interaction of the Adaptor Protein Shc and the Adhesion Molecule Cadherin* , 1997, The Journal of Biological Chemistry.

[16]  Tony Pawson,et al.  The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein–protein interactions , 1996, Current Biology.

[17]  S. Fesik,et al.  Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[18]  B. Margolis,et al.  Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (*) , 1996, The Journal of Biological Chemistry.

[19]  G. Waksman,et al.  pH‐Dependent self‐association of the Src homology 2 (SH2) domain of the Src homologous and collagen‐like (SHC) protein , 1996, Protein science : a publication of the Protein Society.

[20]  A. Petros,et al.  Structure and ligand recognition of the phosphotyrosine binding domain of Shc , 1995, Nature.

[21]  T. Logan,et al.  Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[22]  A. Craparo,et al.  Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain , 1995, Molecular and cellular biology.

[23]  J. Olefsky,et al.  Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. , 1994, The Journal of biological chemistry.

[24]  T Pawson,et al.  Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav , 1994, Molecular and cellular biology.

[25]  A. Ullrich,et al.  Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex. , 1993, The Journal of biological chemistry.

[26]  L. Cantley,et al.  Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. , 1993, Science.

[27]  Sheila M. Thomas,et al.  Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases , 1992, Nature.

[28]  T. Pawson,et al.  A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction , 1992, Cell.