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Biochim Biophys Acta. 2014 Aug;1844(8):1335-43. doi: 10.1016/j.bbapap.2014.03.007. Epub 2014 Mar 19.

Thiol-based redox switches.

Author information

1
Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
2
Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: ujakob@umich.edu.

Abstract

Regulation of protein function through thiol-based redox switches plays an important role in the response and adaptation to local and global changes in the cellular levels of reactive oxygen species (ROS). Redox regulation is used by first responder proteins, such as ROS-specific transcriptional regulators, chaperones or metabolic enzymes to protect cells against mounting levels of oxidants, repair the damage and restore redox homeostasis. Redox regulation of phosphatases and kinases is used to control the activity of select eukaryotic signaling pathways, making reactive oxygen species important second messengers that regulate growth, development and differentiation. In this review we will compare different types of reversible protein thiol modifications, elaborate on their structural and functional consequences and discuss their role in oxidative stress response and ROS adaptation. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.

KEYWORDS:

Disulfide bond; Oxidative stress; Redox regulation; Sulfenic acid

PMID:
24657586
PMCID:
PMC4059413
DOI:
10.1016/j.bbapap.2014.03.007
[Indexed for MEDLINE]
Free PMC Article

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