Tyrosine phosphorylation of NEDD4 activates its ubiquitin ligase activity-Reference-Cited by-同舟云学术

Tyrosine phosphorylation of NEDD4 activates its ubiquitin ligase activity

Published:2014-10-07 Issue:346 Volume:7 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Persaud Avinash¹,Alberts Philipp¹,Mari Sara²,Tong Jiefei³,Murchie Ryan¹,Maspero Elena²,Safi Frozan¹,Moran Michael F.³,Polo Simona²⁴,Rotin Daniela¹

Affiliation:

1. Cell Biology Program, The Hospital for Sick Children, and Biochemistry Department, University of Toronto, 686 Bay Street, Toronto, Ontario M5G 0A4, Canada.

2. IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Via Adamello 16, Milan 20139, Italy.

3. Molecular Structure and Function Program, The Hospital for Sick Children, and Molecular Genetics Department, University of Toronto, Toronto, Ontario M5G 0A4, Canada.

4. Dipartimento Scienze della Salute, Universita degli Studi di Milano, Via di Rudini 8, Milan 20142, Italy.

Abstract

The receptor tyrosine kinases FGFR1 and EGFR promote phosphorylation of the ubiquitin ligase NEDD4, leading to activation of its catalytic activity.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Structure of the FGF Receptor Tyrosine Kinase Domain Reveals a Novel Autoinhibitory Mechanism

2. Cell Signaling by Receptor Tyrosine Kinases

3. Fibroblast growth factor signalling: from development to cancer

4. Ubiquitin in trafficking: The network at work

5. Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function

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