Format

Send to

Choose Destination
See comment in PubMed Commons below
Antioxid Redox Signal. 2011 Mar 1;14(5):757-66. doi: 10.1089/ars.2010.3773. Epub 2011 Jan 4.

Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?

Author information

1
Immunology Program, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY 10065, USA.

Abstract

Protein kinase C (PKC) is activated by lipid second messengers or redox action, raising the question whether these activation modes involve the same or alternate mechanisms. Here we show that both lipid activators and oxidation target the zinc-finger domains of PKC, suggesting a unifying activation mechanism. We found that lipid agonist-binding or redox action leads to zinc release and disassembly of zinc fingers, thus triggering large-scale unfolding that underlies conversion to the active enzyme. These results suggest that PKC zinc fingers, originally considered purely structural devices, are in fact redox-sensitive flexible hinges, whose conformation is controlled both by redox conditions and lipid agonists.

PMID:
21067413
PMCID:
PMC3030452
DOI:
10.1089/ars.2010.3773
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Mary Ann Liebert, Inc. Icon for PubMed Central
    Loading ...
    Support Center