Fas-induced caspase denitrosylation

Joan B. Mannick, Alfred Hausladen, Limin Liu, Douglas T. Hess, Ming Zeng, Qian X. Miao, Laurie S. Kane, Andrew J. Gow, Jonathan S. Stamler

Research output: Contribution to journalArticlepeer-review

683 Citations (Scopus)

Abstract

Only a few intracellular S-nitrosylated proteins have been identified, and it is unknown if protein 5-nitrosylation/denitrosylation is a component of signal transduction cascades. Caspase-3 zymogens were found to be S- nitrosylated on their catalytic-site cysteine in unstimulated human cell tines and denitrosylated upon activation of the Fas apoptotic pathway. Decreased caspase-3 S-nitrosylation was associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active-site thiol. Protein S- nitrosylation/denitrosylation can thus serve as a regulatory process in signal transduction pathways.

Original languageEnglish
Pages (from-to)651-654
Number of pages4
JournalScience
Volume284
Issue number5414
DOIs
Publication statusPublished - 23 Apr 1999
Externally publishedYes

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Fas-induced caspase denitrosylation'. Together they form a unique fingerprint.

Cite this