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Isoform-specific cleavage of 14-3-3 proteins in apoptotic JURL-MK1 cells

✍ Scribed by Kateřina Kuželová; Dana Grebeňová; Michaela Pluskalová; Daniel Kavan; Petr Halada; Zbyněk Hrkal

Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 314 KB
Volume: 106
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.22061

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✦ Synopsis

Abstract

The proteins of 14‐3‐3 family are substantially involved in the regulation of many biological processes including the apoptosis. We studied the changes in the expression of five 14‐3‐3 isoforms (β, γ, ε, τ, and ζ) during the apoptosis of JURL‐MK1 and K562 cells. The expression level of all these proteins markedly decreased in relation with the apoptosis progression and all isoforms underwent truncation, which probably corresponds to the removal of several C‐terminal amino acids. The observed 14‐3‐3 modifications were partially blocked by caspase‐3 inhibition. In addition to caspases, a non‐caspase protease is likely to contribute to 14‐3‐3's cleavage in an isoform‐specific manner. While 14‐3‐3 γ seems to be cleaved mainly by caspase‐3, the alternative mechanism is essentially involved in the case of 14‐3‐3 τ, and a combined effect was observed for the isoforms ε, β, and ζ. We suggest that the processing of 14‐3‐3 proteins could form an integral part of the programmed cell death or at least of some apoptotic pathways. J. Cell. Biochem. 106: 673–681, 2009. © 2009 Wiley‐Liss, Inc.

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