scholarly journals Hepatocyte Growth Factor-regulated Tyrosine Kinase Substrate (HRS) Mediates Post-endocytic Trafficking of Protease-activated Receptor 2 and Calcitonin Receptor-like Receptor

2007 ◽  
Vol 282 (40) ◽  
pp. 29646-29657 ◽  
Author(s):  
Burcu Hasdemir ◽  
Nigel W. Bunnett ◽  
Graeme S. Cottrell
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Endocytic Trafficking ◽  
Calcitonin Receptor ◽  
Kinase Substrate ◽  
Protease Activated Receptor 2 ◽  
Hepatocyte Growth ◽  
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

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 Beclin 1 Promotes Endosome Recruitment of Hepatocyte Growth Factor Tyrosine Kinase Substrate to Suppress Tumor Proliferation

2019 ◽  
Vol 80 (2) ◽  
pp. 249-262 ◽  
Author(s):  
Asia N. Matthew-Onabanjo ◽  
Jenny Janusis ◽  
Jose Mercado-Matos ◽  
Anne E. Carlisle ◽  
Dohoon Kim ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Beclin 1 ◽  
Tumor Proliferation ◽  
Kinase Substrate ◽  
Hepatocyte Growth ◽  
Tyrosine Kinase Substrate

scholarly journals Hepatocyte Growth Factor-regulated Tyrosine Kinase Substrate (HRS) Interacts with PELP1 and Activates MAPK

2006 ◽  
Vol 281 (7) ◽  
pp. 4395-4403 ◽  
Author(s):  
Suresh K. Rayala ◽  
Petra den Hollander ◽  
Seetharaman Balasenthil ◽  
Poonam R. Molli ◽  
Andrew J. Bean ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Kinase Substrate ◽  
Hepatocyte Growth ◽  
Tyrosine Kinase Substrate
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