PMID- 24282406
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20131127
LR  - 20220310
IS  - 1664-462X (Print)
IS  - 1664-462X (Electronic)
IS  - 1664-462X (Linking)
VI  - 4
DP  - 2013
TI  - Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting 
      properties.
PG  - 450
LID - 10.3389/fpls.2013.00450 [doi]
LID - 450
AB  - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved 
      in glycolysis and shown, particularly in animal cells, to play additional roles 
      in several unrelated non-metabolic processes such as control of gene expression 
      and apoptosis. This functional versatility is regulated, in part at least, by 
      redox post-translational modifications that alter GAPDH catalytic activity and 
      influence the subcellular localization of the enzyme. In spite of the well 
      established moonlighting (multifunctional) properties of animal GAPDH, little is 
      known about non-metabolic roles of GAPDH in plants. Plant cells contain several 
      GAPDH isoforms with different catalytic and regulatory properties, located both 
      in the cytoplasm and in plastids, and participating in glycolysis and the 
      Calvin-Benson cycle. A general feature of all GAPDH proteins is the presence of 
      an acidic catalytic cysteine in the active site that is overly sensitive to 
      oxidative modifications, including glutathionylation and S-nitrosylation. In 
      Arabidopsis, oxidatively modified cytoplasmic GAPDH has been successfully used as 
      a tool to investigate the role of reduced glutathione, thioredoxins and 
      glutaredoxins in the control of different types of redox post-translational 
      modifications. Oxidative modifications inhibit GAPDH activity, but might enable 
      additional functions in plant cells. Mounting evidence support the concept that 
      plant cytoplasmic GAPDH may fulfill alternative, non-metabolic functions that are 
      triggered by redox post-translational modifications of the protein under stress 
      conditions. The aim of this review is to detail the molecular mechanisms 
      underlying the redox regulation of plant cytoplasmic GAPDH in the light of its 
      crystal structure, and to provide a brief inventory of the well known 
      redox-dependent multi-facetted properties of animal GAPDH, together with the 
      emerging roles of oxidatively modified GAPDH in stress signaling pathways in 
      plants.
FAU - Zaffagnini, Mirko
AU  - Zaffagnini M
AD  - Laboratory of Plant Redox Biology, Department of Pharmacy and Biotechnology, 
      University of Bologna Bologna, Italy.
FAU - Fermani, Simona
AU  - Fermani S
FAU - Costa, Alex
AU  - Costa A
FAU - Lemaire, Stephane D
AU  - Lemaire SD
FAU - Trost, Paolo
AU  - Trost P
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20131112
PL  - Switzerland
TA  - Front Plant Sci
JT  - Frontiers in plant science
JID - 101568200
PMC - PMC3824636
OTO - NOTNLM
OT  - S-nitrosylation
OT  - cysteine thiols
OT  - glycolytic glyceraldehyde-3-phosphate dehydrogenase
OT  - moonlighting protein
OT  - redox modifications
EDAT- 2013/11/28 06:00
MHDA- 2013/11/28 06:01
PMCR- 2013/01/01
CRDT- 2013/11/28 06:00
PHST- 2013/09/30 00:00 [received]
PHST- 2013/10/21 00:00 [accepted]
PHST- 2013/11/28 06:00 [entrez]
PHST- 2013/11/28 06:00 [pubmed]
PHST- 2013/11/28 06:01 [medline]
PHST- 2013/01/01 00:00 [pmc-release]
AID - 10.3389/fpls.2013.00450 [doi]
PST - epublish
SO  - Front Plant Sci. 2013 Nov 12;4:450. doi: 10.3389/fpls.2013.00450. eCollection 
      2013.