A SECRETED TYROSINE KINASE ACTS IN THE EXTRACELLULAR ENVIRONMENT
| Autor: | Swee Kee Wong, Maja Edenius, Joseph E. Italiano, John M. Asara, Jonathan N. Thon, Mattia Renato Bordoli, Tracy Keller, Jina Yum, Carolyn A. Worby, Susanne B. Breitkopf, Grace Lin, Chang Yeol Yeo, Jack E. Dixon, Junyu Xiao, Malcolm Whitman |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Blood Platelets
Glycosylation Molecular Sequence Data Embryonic Development Protein tyrosine phosphatase SH2 domain Receptor tyrosine kinase General Biochemistry Genetics and Molecular Biology Article Mice chemistry.chemical_compound 03 medical and health sciences 0302 clinical medicine Animals Humans Amino Acid Sequence Phosphorylation Tyrosine 030304 developmental biology 0303 health sciences Secretory Pathway biology Biochemistry Genetics and Molecular Biology(all) Tyrosine phosphorylation Protein-Tyrosine Kinases Embryo Mammalian Protein Structure Tertiary Cell biology chemistry Biochemistry ROR1 biology.protein Protein Processing Post-Translational Protein Kinases Platelet-derived growth factor receptor 030217 neurology & neurosurgery Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | CELL |
| Popis: | SummaryAlthough tyrosine phosphorylation of extracellular proteins has been reported to occur extensively in vivo, no secreted protein tyrosine kinase has been identified. As a result, investigation of the potential role of extracellular tyrosine phosphorylation in physiological and pathological tissue regulation has not been possible. Here, we show that VLK, a putative protein kinase previously shown to be essential in embryonic development, is a secreted protein kinase, with preference for tyrosine, that phosphorylates a broad range of secreted and ER-resident substrate proteins. We find that VLK is rapidly and quantitatively secreted from platelets in response to stimuli and can tyrosine phosphorylate coreleased proteins utilizing endogenous as well as exogenous ATP sources. We propose that discovery of VLK activity provides an explanation for the extensive and conserved pattern of extracellular tyrosine phosphophorylation seen in vivo, and extends the importance of regulated tyrosine phosphorylation into the extracellular environment.PaperClip |
| Databáze: | OpenAIRE |
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