scholarly journals Substrate binding to Src: A new perspective on tyrosine kinase substrate recognition from NMR and molecular dynamics

2019 ◽  
Vol 29 (2) ◽  
pp. 350-359 ◽  
Author(s):  
Mehul K. Joshi ◽  
Robert A. Burton ◽  
Heng Wu ◽  
Andrew M. Lipchik ◽  
Barbara P. Craddock ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Tyrosine Kinase ◽  
Substrate Binding ◽  
Substrate Recognition ◽  
Kinase Substrate ◽  
New Perspective ◽  
Tyrosine Kinase Substrate

Hepatocyte growth factor-regulated tyrosine kinase substrate (HGS) and guanylate kinase 1 (GUK1) are differentially expressed in GH-secreting adenomas

Pituitary ◽  
2006 ◽  
Vol 9 (2) ◽  
pp. 83-92 ◽  
Author(s):  
Anderson Alves da Rocha ◽  
Ricardo Rodrigues Giorgi ◽  
Sandra Valeria de Sa ◽  
Maria Lucia Correa-Giannella ◽  
Maria Angela Fortes ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Differentially Expressed ◽  
Guanylate Kinase ◽  
Kinase Substrate ◽  
Hepatocyte Growth ◽  
Tyrosine Kinase Substrate

Angiostatin Binds to Tyrosine Kinase Substrate Annexin II through the Lysine-Binding Domain in Endothelial Cells

2002 ◽  
Vol 64 (3) ◽  
pp. 448-462 ◽  
Author(s):  
George P. Tuszynski ◽  
Meena R. Sharma ◽  
Vicki L. Rothman ◽  
Mahesh C. Sharma
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Kinase ◽  
Binding Domain ◽  
Annexin Ii ◽  
Kinase Substrate ◽  
Tyrosine Kinase Substrate

scholarly journals Endosomal Localization and Receptor Dynamics Determine Tyrosine Phosphorylation of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate

2000 ◽  
Vol 20 (20) ◽  
pp. 7685-7692 ◽  
Author(s):  
Sylvie Urbé ◽  
Ian G. Mills ◽  
Harald Stenmark ◽  
Naomi Kitamura ◽  
Michael J. Clague
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Membrane Trafficking ◽  
Signal Transduction Pathway ◽  
Dominant Negative ◽  
Kinase Substrate ◽  
Hepatocyte Growth ◽  
Tyrosine Kinase Substrate

ABSTRACT Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) is a prominent substrate for activated tyrosine kinase receptors that has been proposed to play a role in endosomal membrane trafficking. The protein contains a FYVE domain, which specifically binds to the lipid phosphatidylinositol (PI) 3-phosphate (PI 3-P). We show that this interaction is required both for correct localization of the protein to endosomes that only partially coincides with early endosomal autoantigen 1 and for efficient tyrosine phosphorylation of the protein in response to epidermal growth factor stimulation. Treatment with wortmannin reveals that Hrs phosphorylation also requires PI 3-kinase activity, which is necessary to generate the PI 3-P required for localization. We have used both hypertonic media and expression of a dominant-negative form of dynamin (K44A) to inhibit endocytosis; under which conditions, receptor stimulation fails to elicit phosphorylation of Hrs. Our results provide a clear example of the coupling of a signal transduction pathway to endocytosis, from which we propose that activated receptor (or associated factor) must be delivered to the appropriate endocytic compartment in order for Hrs phosphorylation to occur.

scholarly journals The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein.

1986 ◽  
Vol 102 (2) ◽  
pp. 660-669 ◽  
Author(s):  
K L Gould ◽  
J A Cooper ◽  
A Bretscher ◽  
T Hunter
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Immunofluorescent Staining ◽  
Soluble Form ◽  
Cell Fractionation ◽  
A431 Cells ◽  
Protein Tyrosine ◽  
Kinase Substrate ◽  
Core Proteins ◽  
Tyrosine Kinase Substrate

p81, a protein-tyrosine kinase substrate previously identified in epidermal growth factor-treated A431 cells, is demonstrated to be homologous to ezrin, an 80-kD component of microvillar core proteins. p81 has been characterized using antiserum raised against purified chicken intestinal ezrin. p81, located by indirect immunofluorescent staining, is concentrated in surface projections of A431 cells such as microvilli and retraction fibers. None of the conditions of biochemical cell fractionation tested completely solubilizes p81; the insoluble p81 partitions as if associated with the cytoskeleton. The soluble form of p81 behaves as a monomer in all extraction procedures studied. EGF-stimulated phosphorylation of p81 does not appear to change its intracellular location. p81 exhibits a wide tissue distribution with highest levels of expression in small intestine, kidney, thymus, and lung. Intermediate levels are found in spleen, thymus, lymph nodes, and bone marrow, with low levels in brain, heart, and testes. p81 is undetectable in muscle and liver. In A431 cells, p81 is phosphorylated on serine and threonine residues. Upon EGF treatment, approximately 10% of p81 becomes phosphorylated on tyrosine, and the phosphorylation of threonine residues increases.

scholarly journals Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLCγ1

2009 ◽  
Vol 106 (50) ◽  
pp. 21143-21148 ◽  
Author(s):  
Lie Min ◽  
Raji E. Joseph ◽  
D. Bruce Fulton ◽  
Amy H. Andreotti
Keyword(s):  
Tyrosine Kinase ◽  
Sh2 Domain ◽  
Kinase Substrate ◽  
Substrate Docking ◽  
Tyrosine Kinase Substrate

Conformational Studies on Calcium Binding BytBoc-Leu-Pro-Tyr-Ala-NHCH3, a Tyrosine Kinase Substrate, in a Nonpolar Solvent

1993 ◽  
Vol 11 (3) ◽  
pp. 509-528 ◽  
Author(s):  
Vettai S. Ananthanarayanan ◽  
Andre Saint-Jean ◽  
Bruce V. Cheesman ◽  
Donald W. Hughes ◽  
Alex D. Bain
Keyword(s):  
Tyrosine Kinase ◽  
Calcium Binding ◽  
Nonpolar Solvent ◽  
Conformational Studies ◽  
Kinase Substrate ◽  
Tyrosine Kinase Substrate
Sign in / Sign up

Export Citation Format

Share Document