Format

Send to

Choose Destination
J Biol Chem. 2013 Dec 6;288(49):35117-25. doi: 10.1074/jbc.M113.521443. Epub 2013 Oct 16.

Identification of a dithiol-disulfide switch in collapsin response mediator protein 2 (CRMP2) that is toggled in a model of neuronal differentiation.

Author information

1
From the Institute for Medical Biochemistry and Molecular Biology, University Medicine, Ernst-Moritz-Arndt-University Greifswald, 17475 Greifswald, Germany and.

Abstract

Vertebrate-specific glutaredoxin 2 (Grx2) is expressed in at least two isoforms, mitochondrial Grx2a and cytosolic Grx2c. We have previously shown that cytosolic Grx2 is essential for embryonic development of the brain. In particular, we identified collapsin response mediator protein 2 (CRMP2/DPYSL2), a mediator of the semaphorin-plexin signaling pathway, as redox-regulated target of Grx2c and demonstrated that this regulation is required for normal axonal outgrowth. In this study, we demonstrate the molecular mechanism of this regulation, a specific and reversible intermolecular Cys-504-Cys-504 dithiol-disulfide switch in homotetrameric CRMP2. This switch determines two conformations of the quaternary CRMP2 complex that controls axonal outgrowth and thus neuronal development.

KEYWORDS:

CRMP2; Disulfide; Glutaredoxin; Neurodifferentiation; Neuronal Differentiation; Redox Regulation; Redox Signaling; Redox Switch; Thiol

PMID:
24133216
PMCID:
PMC3853263
DOI:
10.1074/jbc.M113.521443
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center