國家衛生研究院 NHRI:Item 3990099045/2263

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Title:	Proteolytic activation of Etk/Bmx tyrosine kinase by caspases
Authors:	Wu, YM;Huang, CL;Kung, HJ;Huang, CYF
Contributors:	Division of Molecular and Genomic Medicine
Abstract:	Etk/Bmx is a member of the Btk/Tec family of kinases, which are characterized by having a pleckstrin homology domain at the N terminus, in addition to the Src homology 3 (SH3), SH2, and the catalytic domains, shared with the Src family kinases, Etk, or Btk kinases in general, has been implicated in the regulation of apoptosis. To test whether Etk is the substrate for caspases during apoptosis, in vitro translated [S-35]methionine-labeled Etk was incubated with different apoptotic extracts and recombinant caspases, respectively. Results showed that Etk was proteolyzed in all conditions tested with identical cleavage patterns. Caspase-mediated cleavage of Etk generated a C-terminal fragment, containing the complete SH2 and tyrosine kinase domains, but without intact pleckstrin homology and SH3 domains. This fragment has 4-fold higher kinase activity than that of the full-length Etk, Ectopic expression of the C-terminal fragment of Etk sensitized the PC3 prostate cancer cells to apoptosis in response to apoptosis-inducing stimuli. The finding, together with an earlier report that Etk is potentially anti-apoptotic, suggests that Etk may serve as an apoptotic switch, depending on the forms of Etk existing inside the cells. To our knowledge, this is the first case where the activity of a tyrosine kinase is induced by caspase cleavage.
Keywords:	Biochemistry & Molecular Biology
Date:	2001-05-25
Relation:	Journal of Biological Chemistry. 2001 May;276(21):17672-17678.
Link to:	http://dx.doi.org/10.1074/jbc.M010964200
JIF/Ranking 2023:	http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=1083-351X&DestApp=IC2JCR
Cited Times(WOS):	https://www.webofscience.com/wos/woscc/full-record/WOS:000168866500008
Cited Times(Scopus):	http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035947704
Appears in Collections:	[Chi-Ying F. Huang(1998-2005)] Periodical Articles [Hsing-Jien Kung] Periodical Articles

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