SHIP1, an SH2 Domain Containing Polyinositol-5-phosphatase, Regulates Migration through Two Critical Tyrosine Residues and Forms a Novel Signaling Complex with DOK1 and CRKL
Open Access
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (4) , 2451-2458
- https://doi.org/10.1074/jbc.m006250200
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Molecular Cloning and Characterization of p56 Defines a New Family of RasGAP-binding ProteinsJournal of Biological Chemistry, 1998
- Identification of a Second SH2-Domain-Containing Protein Closely Related to the Phosphatidylinositol Polyphosphate 5-Phosphatase SHIPBiochemical and Biophysical Research Communications, 1997
- Differential Signaling after β1 Integrin Ligation Is Mediated Through Binding of CRKL to p120 and p110Published by Elsevier ,1997
- Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIPPublished by Elsevier ,1997
- Activation of hematopoietic growth factor signal transduction pathways by the human oncogene BCR/ABLCytokine & Growth Factor Reviews, 1997
- Structure of the IRS-1 PTB Domain Bound to the Juxtamembrane Region of the Insulin ReceptorPublished by Elsevier ,1996
- Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2Current Biology, 1996
- Structure and ligand recognition of the phosphotyrosine binding domain of ShcNature, 1995
- Cloning and Characterization of a Human cDNA (INPPL1) Sharing Homology with Inositol Polyphosphate PhosphatasesGenomics, 1995
- The chemotactic response to PDGF-BB: evidence of a role for Ras.The Journal of cell biology, 1995