Caveolin-1 is Transiently Dephosphorylated by Shear Stress-activated Protein Tyrosine Phosphatase Mu.
From: Department of Molecular Biology and Institute of Nanosensor and Biotechnology, Dankook University, San 8, Hannam-dong, Yongsan-ku, Seoul 140-714, Republic of Korea.
Biochemical and biophysical research communications
- Publish Date: Jan 2006
- ISSN: 0006-291X
- Volume: 339
- Issue: 3
- Pages: 737-41
- Medium: Print
- Language: English
- Citation (JAMA): Shin Jaeyoung, Jo Hanjoong, Park Heonyong, et al. Caveolin-1 is Transiently Dephosphorylated by Shear Stress-activated Protein Tyrosine Phosphatase Mu.. Biochem. Biophys. Res. Commun. Jan 2006;339:737-41
Abstract
Endothelial cells are subjected to hemodynamic shear stress, which regulates multiple vascular functions partially by the caveolin-1-dependent mechanisms. Caveolin-1 is a principal protein in the plasma membrane microdomains called caveolae and interacts with various signaling molecules. Recently, caveolin-1 was elucidated to be phosphorylated on tyrosine 14. However, it is not known how phosphorylation of caveolin-1 is controlled in endothelium. In this study, we found that caveolin-1 is phosphorylated by p38 mitogen-activated protein kinase (MAPK) under a static condition. When endothelial cells were exposed to shear stress, caveolin-1 was transiently dephosphorylated. Since the activity of p38 MAPK was not affected by shear stress, the shear-dependent dephosphorylation of caveolin-1 was not mediated by p38 MAPK. Of interest, sodium orthovanadate, an inhibitor for phosphatases, blocked the shear-dependent dephosphorylation of caveolin-1. We also observed that protein tyrosine phosphatase mu was transiently activated by shear stress, suggesting its role in the dephosphorylation of caveolin-1.
Mesh Headings (Keywords): Animals, Cattle, Caveolin 1, Cells, Cultured, Endothelial Cells, Kinetics, Mechanotransduction, Cellular, Phosphorylation, Protein Tyrosine Phosphatases, Receptor-Like Protein Tyrosine Phosphatases, Class 2, Shear Strength, Stress, Mechanical, Time Factors, p38 Mitogen-Activated Protein Kinases
Check for Full Text / PubMed Unique Identifier (PMID): 16325778
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.