ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
Author:
Affiliation:
1. Instituto de Investigaciones Biotecnológicas, IIB-INTECH, Universidad de San Martín, 1650 San Martín, Buenos Aires, Argentina
2. Department of Biological Sciences, University of Iowa, Iowa City, IA 52242, USA
Abstract
Publisher
The Company of Biologists
Subject
Cell Biology
Link
http://journals.biologists.com/jcs/article-pdf/119/7/1233/1511727/1233.pdf
Reference62 articles.
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2. Arregui, C. O., Balsamo, J. and Lilien, J. (2000). Regulation of signaling by protein-tyrosine phosphatases: Potential roles in the nervous system. Neurochem. Res.25, 95-105.
3. Balsamo, J., Arregui, C., Leung, T. C. and Lilien, J. (1998). The nonreceptor protein tyrosine phosphatase PTP1B binds to the cytoplasmic domain of N-cadherin and regulates the cadherin-actin linkage. J. Cell Biol.143, 523-532.
4. Bjorge, J. D., Pang, A. and Fujita, D. J. (2000). Identification of protein tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem.275, 41439-41446.
5. Bhatt, A., Kaverina, I., Otey, C. and Huttenlocher, A. (2002). Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J. Cell Sci.115, 3415-3425.
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