Linked Life Data

20601085

Source:http://linkedlifedata.com/resource/pubmed/id/20601085

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-8-30
pubmed:abstractText
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is considered a housekeeping glycolitic enzyme that recently has been implicated in cell signaling. Under apoptotic stresses, cells activate nitric oxide formation leading to S-nitrosylation of GAPDH that binds to Siah and translocates to the nucleus. The GAPDH-Siah interaction depends on the integrity of lysine 227 in human GAPDH, being the mutant K227A unable to associate with Siah. As lysine residues are susceptible to be modified by acetylation, we aimed to analyze whether acetylation could mediate transport of GAPDH from cytoplasm to the nucleus. We observed that the acetyltransferase P300/CBP-associated factor (PCAF) interacts with and acetylates GAPDH. We also found that over-expression of PCAF induces the nuclear translocation of GAPDH and that for this translocation its intact acetylase activity is needed. Finally, the knocking down of PCAF reduces nuclear translocation of GAPDH induced by apoptotic stimuli. By spot mapping analysis we first identified Lys 117 and 251 as the putative GAPDH residues that could be acetylated by PCAF. We further demonstrated that both Lys were necessary but not sufficient for nuclear translocation of GAPDH after apoptotic stimulation. Finally, we identified Lys 227 as a third GAPDH residue whose acetylation is needed for its transport from cytoplasm to the nucleus. Thus, results reported here indicate that nuclear translocation of GAPDH is mediated by acetylation of three specific Lys residues (117, 227 and 251 in human cells). Our results also revealed that PCAF participates in the GAPDH acetylation that leads to its translocation to the nucleus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1878-5875
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1672-80
pubmed:meshHeading
pubmed-meshheading:20601085-Acetylation, pubmed-meshheading:20601085-Active Transport, Cell Nucleus, pubmed-meshheading:20601085-Animals, pubmed-meshheading:20601085-Apoptosis, pubmed-meshheading:20601085-Cell Nucleus, pubmed-meshheading:20601085-Cloning, Molecular, pubmed-meshheading:20601085-Glyceraldehyde-3-Phosphate Dehydrogenases, pubmed-meshheading:20601085-Humans, pubmed-meshheading:20601085-Lysine, pubmed-meshheading:20601085-Mice, pubmed-meshheading:20601085-Mutation, pubmed-meshheading:20601085-NIH 3T3 Cells, pubmed-meshheading:20601085-Nuclear Proteins, pubmed-meshheading:20601085-Protein Binding, pubmed-meshheading:20601085-RNA, Small Interfering, pubmed-meshheading:20601085-Signal Transduction, pubmed-meshheading:20601085-Ubiquitin-Protein Ligases, pubmed-meshheading:20601085-p300-CBP Transcription Factors
pubmed:year
2010
pubmed:articleTitle
Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase is regulated by acetylation.
pubmed:affiliation
Department of Cell Biology, Immunology and Neurosciences, Faculty of Medicine, University of Barcelona, Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't