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  Regulation of Signaling at Regions of Cell-Cell Contact by Endoplasmic Reticulum-Bound Protein-Tyrosine Phosphatase 1B

Haj, F. G., Sabet, O., Kinkhabwala, A., Wimmer-Kleikamp, S., Roukos, V., Han, H., et al. (2012). Regulation of Signaling at Regions of Cell-Cell Contact by Endoplasmic Reticulum-Bound Protein-Tyrosine Phosphatase 1B. PLoS ONE, 7(5): e36633. Retrieved from http://dx.doi.org/10.1371/journal.pone.0036633.

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 Creators:
Haj, Fawaz G.1, Author
Sabet, Ola2, Author              
Kinkhabwala, Ali2, Author              
Wimmer-Kleikamp, Sabine2, Author
Roukos, Vassilis2, Author
Han, Hongmei2, Author              
Grabenbauer, Markus2, Author              
Bierbaum, Martin2, Author              
Antony, Claude3, Author
Neel, Benjamin G.1, Author
Bastiaens, Philippe I.2, Author              
Affiliations:
1Beth Israel Deaconess Medical Center, Harvard University, Boston, Massachusetts, United States of America, ou_persistent22              
2Abt. II: Systemische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753288              
3European Molecular Biology Laboratories, Heidelberg, Germany, ou_persistent22              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2012-05-24
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 611011
URI: http://dx.doi.org/10.1371/journal.pone.0036633
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Title: PLoS ONE
Source Genre: Journal
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Pages: - Volume / Issue: 7 (5) Sequence Number: e36633 Start / End Page: - Identifier: -