Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Support Wiki
Direct access to
document ID:

          Document History for Document ID 611011

Back to latest document version
Document Version Version Comment Date Status
611011.0 [No comment] 30.07.2012 13:45 Released

ID: 611011.0, MPI für molekulare Physiologie / Abteilung II - Systemische Zellbiologie
Regulation of Signaling at Regions of Cell-Cell Contact by Endoplasmic Reticulum-Bound Protein-Tyrosine Phosphatase 1B
Authors:Haj, Fawaz G.; Sabet, Ola; Kinkhabwala, Ali; Wimmer-Kleikamp, Sabine; Roukos, Vassilis; Han, Hong-Mei; Grabenbauer, Markus; Bierbaum, Martin; Antony, Claude; Neel, Benjamin G.; Bastiaens, Philippe I.
Date of Publication (YYYY-MM-DD):2012-05-24
Title of Journal:PLoS ONE
Issue / Number:5
Sequence Number of Article:e36633
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Protein-tyrosine phosphatase 1B (PTP1B) is a ubiquitously expressed PTP that is anchored to the endoplasmic reticulum (ER). PTP1B dephosphorylates activated receptor tyrosine kinases after endocytosis, as they transit past the ER. However, PTP1B also can access some plasma membrane (PM)-bound substrates at points of cell-cell contact. To explore how PTP1B interacts with such substrates, we utilized quantitative cellular imaging approaches and mathematical modeling of protein mobility. We find that the ER network comes in close proximity to the PM at apparently specialized regions of cell-cell contact, enabling PTP1B to engage substrate(s) at these sites. Studies using PTP1B mutants show that the ER anchor plays an important role in restricting its interactions with PM substrates mainly to regions of cell-cell contact. In addition, treatment with PTP1B inhibitor leads to increased tyrosine phosphorylation of EphA2, a PTP1B substrate, specifically at regions of cell-cell contact. Collectively, our results identify PM-proximal sub-regions of the ER as important sites of cellular signaling regulation by PTP1B.
External Publication Status:published
Document Type:Article
Communicated by:Jürgen Block
Affiliations:MPI für molekulare Physiologie/Abteilung II - Systemische Zellbiologie/AG Prof. Dr. P. Bastiaens
MPI für molekulare Physiologie/Abteilung II - Systemische Zellbiologie/AG Dr. A. Kinkhabwala
MPI für molekulare Physiologie/Abteilung II - Systemische Zellbiologie/AG Dr. M. Grabenbauer
Identifiers:URL:http://dx.doi.org/10.1371/journal.pone.0036633 [Article locator with full text links]