• EN
  • DA

Danish NationalResearch Database

  • Publications
  • Researchers
Example Finds records
water{} containing the word "water".
water supplies"{}" containing the phrase "water supplies".
author:"Doe, John"author:"{}" containing the phrase "Doe, John" in the author field.
title:IEEEtitle:{} containing the word "IEEE" in the title field.
bech{} containing the word "bech".
marie bech"{}" containing the phrase "marie bech".
orcid:0000-0002-5429-5292orcid:{} Having a particular ORCID
Need more help? Advanced search tutorial
  • Selected (0)
  • History

PTP1B targets the endosomal sorting machinery

    • Save to Mendeley
    • Export to BibTeX
    • Export to RIS
    • Email citation
Authors:
  • Stuible, Matthew ;
    Close
    unknown
  • Abella, Jasmine V ;
    Close
    unknown
  • Feldhammer, Matthew ;
    Close
    unknown
  • Nossov, Misha ;
    Close
    unknown
  • Sangwan, Veena ;
    Close
    unknown
  • Blagoev, Blagoy ;
    Close
    Orcid logo0000-0002-3596-0066
    Department of Biochemistry and Molecular Biology, Faculty of Science, University of Southern Denmark
  • Park, Morag ;
    Close
    unknown
  • Tremblay, Michel L
    Close
    unknown
Subtitle:
dephosphorylation of regulatory sites on the endosomal sorting complex required for transport component STAM2
DOI:
10.1074/jbc.m110.115295
Abstract:
Dephosphorylation and endocytic down-regulation are distinct processes that together control the signaling output of a variety of receptor tyrosine kinases (RTKs). PTP1B can directly dephosphorylate several RTKs, but it can also promote activation of downstream pathways through largely unknown mechanisms. These positive signaling functions likely contribute to the tumor-promoting effect of PTP1B in mouse cancer models. Here, we have identified STAM2, an endosomal protein involved in sorting activated RTKs for lysosomal degradation, as a substrate of PTP1B. PTP1B interacts with STAM2 at defined phosphotyrosine sites, and knockdown of PTP1B expression augments STAM2 phosphorylation. Intriguingly, manipulating the expression and phosphorylation state of STAM2 did not have a general effect on epidermal growth factor (EGF)-induced EGF receptor trafficking, degradation, or signaling. Instead, phosphorylated STAM2 specifically suppressed Akt activation, and a phosphorylation-deficient STAM2 mutant displayed prolonged localization on endosomes following EGF stimulation. These results reveal a novel link between the dephosphorylation and endocytic machinery and suggest that PTP1B can affect RTK signaling in a previously unrecognized manner.
Type:
Journal article
Language:
English
Published in:
Journal of Biological Chemistry, 2010, Vol 285, Issue 31, p. 23899-907
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2010
Scientific Level:
Scientific
ID:
78304278

Full text access

  • Doi Get publisher edition via DOI resolver
Checking for on-site access...

On-site access

At institution

  • University southern denmark.en
Feedback

Sitemap

  • Search
    • Statistics
    • Tutorial
    • Data
    • FAQ
    • Contact
  • About
    • Institutions
    • Release History
    • Cookies and Personal Data
  • Open Access
    • The Danish Open Access Indicator

Copyright © 1998–2018.

Fivu en