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Determination of the transphosphorylation sites of Jak2 kinase.

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/28122

Title: Determination of the transphosphorylation sites of Jak2 kinase.
Authors: Matsuda, Tadashi Browse this author →KAKEN DB
Feng, Jian Browse this author
Witthuhn, Bruce A. Browse this author
Sekine, Yuichi Browse this author
Ihle, James N. Browse this author
Keywords: Jak
Transphosphorylation
Issue Date: 10-Dec-2004
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 325
Issue: 2
Start Page: 586
End Page: 594
Publisher DOI: 10.1016/j.bbrc.2004.10.071
PMID: 15530433
Abstract: Janus kinases are the key enzymes involved in the initial transmission of signals in response to type I and II cytokines. Activation of the signal begins with the transphosphorylation of Jak kinases. Substrates that give rise to downstream events are recruited to the receptor complex in part by interactions with phosphorylated tyrosines. The identity of many of the phosphotyrosines responsible for recruitment has been elucidated as being receptor-based tyrosines. The ability of Jaks to recruit substrates through their own phosphotyrosines has been demonstrated for tyrosines in the kinase activation loop. Recent studies demonstrate that other tyrosines have implications in regulatory roles of Jak kinase activity. In this study, baculovirus-produced Jak2 was utilized to demonstrate that transphosphorylation of Jak kinases occurs on multiple residues throughout the protein. We demonstrate that among the tyrosines phosphorylated, those in the kinase domain occur as expected, but many other sites are also phosphorylated. The tyrosines conserved in the Jak family are the object of this study, although many of them are phosphorylated, many are not. This result suggests that conservation of tyrosines is perhaps as important in maintaining structure of the Jak family. Additionally, non-Jak family conserved tyrosines are phosphorylated suggesting that the individual Jaks ability to phosphorylated specific tyrosines may influence signals emitting from activated Jaks.
Relation: http://www.sciencedirect.com/science/journal/0006291X
Type: article (author version)
URI: http://hdl.handle.net/2115/28122
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

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