The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617F-positive cells and mediates proliferation of human erythroleukaemia cells-Reference-Cited by-同舟云学术

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The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617F-positive cells and mediates proliferation of human erythroleukaemia cells

Published:2017-07 Issue: Volume:35 Page:37-47
ISSN:0898-6568
Container-title:Cellular Signalling
language:en
Short-container-title:Cellular Signalling

Author:

Bongartz Hannes,Hessenkemper Wiebke,Müller Christian^ORCID,Fensky Melissa,Fritsch Johannes,Mandel Katharina,Behrmann Iris,Haan Claude,Fischer Thomas,Feller Stephan M.,Schaper Fred

Funder

German Federal Ministry for Education and Science

German Federal State of Saxony-Anhalt

Breast Cancer Campaign

Rosetrees Trust

Cancer Research UK

Volkswagen Stiftung

University of Luxembourg

Publisher

Elsevier BV

Subject

Cell Biology

Reference20 articles.

1. Function, regulation and pathological roles of the Gab/DOS docking proteins;Wöhrle;Cell Commun. Signal,2009

2. Coupling of Gab1 to c-Met, Grb2, and Shp2 mediates biological responses;Schaeper;J. Cell Biol.,2000

3. A critical role for phosphoinositide 3-kinase upstream of Gab1 and SHP2 in the activation of ras and mitogen-activated protein kinases by epidermal growth factor;Yart;J. Biol. Chem.,2001

4. Signal strength dictates PI3K contribution to Ras/ERK1-2 activation via differential Gab1/Shp2 recruitment: consequences for resistance to EGFR inhibition;Sampaio;Mol. Cell. Biol.,2007

5. A new mechanism for the regulation of Gab1 recruitment to the plasma membrane;Eulenfeld;J. Cell Sci.,2009

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