| Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells. | |
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MedLine Citation:
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PMID: 12972546 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Platelet endothelial adhesion molecule-1 (PECAM-1) is a part of intercellular junctions and triggers intracellular signaling cascades upon homophilic binding. The intracellular domain of PECAM-1 is tyrosine phosphorylated upon homophilic engagement. However, it remains unclear which tyrosine kinase phosphorylates PECAM-1. We sought to isolate tyrosine kinases responsible for PECAM-1 phosphorylation and identified Fer as a candidate, based on expression cloning. Fer kinase specifically phosphorylated PECAM-1 at the immunoreceptor tyrosine-based inhibitory motif. Notably, Fer induced tyrosine phosphorylation of SHP-2, which is known to bind to the immunoreceptor tyrosine-based inhibitory motif of PECAM-1, and Fer also induced tyrosine phosphorylation of Gab1 (Grb2-associated binder-1). Engagement-dependent PECAM-1 phosphorylation was inhibited by the overexpression of a kinase-inactive mutant of Fer, suggesting that Fer is responsible for the tyrosine phosphorylation upon PECAM-1 engagement. Furthermore, by using green fluorescent protein-tagged Fer and a time-lapse fluorescent microscope, we found that Fer localized at microtubules in polarized and motile vascular endothelial cells. Fer was dynamically associated with growing microtubules in the direction of cell-cell contacts, where p120catenin, which is known to associate with Fer, colocalized with PECAM-1. These results suggest that Fer localized on microtubules may play an important role in phosphorylation of PECAM-1, possibly through its association with p120catenin at nascent cell-cell contacts. |
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Authors:
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Naoko Kogata; Michitaka Masuda; Yuji Kamioka; Akiko Yamagishi; Akira Endo; Masato Okada; Naoki Mochizuki |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2003-06-13 |
Journal Detail:
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Title: Molecular biology of the cell Volume: 14 ISSN: 1059-1524 ISO Abbreviation: Mol. Biol. Cell Publication Date: 2003 Sep |
Date Detail:
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Created Date: 2003-09-15 Completed Date: 2004-04-08 Revised Date: 2010-01-29 |
Medline Journal Info:
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Nlm Unique ID: 9201390 Medline TA: Mol Biol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 3553-64 Citation Subset: IM |
Affiliation:
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Department of Structural Analysis, National Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing Animals Antigens, CD31 / metabolism*, physiology Cattle Cell Adhesion / physiology Cell Adhesion Molecules / metabolism, physiology Cells, Cultured Cloning, Molecular Endothelial Cells / enzymology*, physiology Gene Library Green Fluorescent Proteins Humans Intracellular Signaling Peptides and Proteins Luminescent Proteins Microtubules / enzymology*, metabolism, physiology Mutation Phosphoproteins / metabolism*, physiology Phosphorylation Protein Structure, Tertiary Protein Tyrosine Phosphatase, Non-Receptor Type 11 Protein Tyrosine Phosphatases / metabolism, physiology Protein-Tyrosine Kinases Proto-Oncogene Proteins / metabolism*, physiology |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/Antigens, CD31; 0/Cell Adhesion Molecules; 0/GAB1 protein, human; 0/Intracellular Signaling Peptides and Proteins; 0/Luminescent Proteins; 0/Phosphoproteins; 0/Proto-Oncogene Proteins; 0/delta catenin; 110736-90-8/proto-oncogene protein c-fes-fps; 147336-22-9/Green Fluorescent Proteins; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 3.1.3.48/PTPN11 protein, human; EC 3.1.3.48/Protein Tyrosine Phosphatase, Non-Receptor Type 11; EC 3.1.3.48/Protein Tyrosine Phosphatases |
| Comments/Corrections | |
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