Document Detail


Loss of the VHR dual-specific phosphatase causes cell-cycle arrest and senescence.
MedLine Citation:
PMID:  16604064     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein tyrosine phosphatases regulate important processes in eukaryotic cells and have critical functions in many human diseases including diabetes to cancer. Here, we report that the human Vaccinia H1-related (VHR) dual-specific protein tyrosine phosphatase regulates cell-cycle progression and is itself modulated during the cell cycle. Using RNA interference (RNAi), we demonstrate that cells lacking VHR arrest at the G1-S and G2-M transitions of the cell cycle and show the initial signs of senescence, such as flattening, spreading, appearance of autophagosomes, beta-galactosidase staining and decreased telomerase activity. In agreement with this notion, cells lacking VHR were found to upregulate p21(Cip-Waf1), whereas they downregulated the expression of genes for cell-cycle regulators, DNA replication, transcription and mRNA processing. Loss of VHR also caused a several-fold increase in serum-induced activation of its substrates, the mitogen-activated protein (MAP) kinases Jnk and Erk. VHR-induced cell-cycle arrest was dependent on this hyperactivation of Jnk and Erk, and was reversed by Jnk and Erk inhibition or knock-down. We conclude that VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner.
Authors:
Souad Rahmouni; Fabio Cerignoli; Andres Alonso; Toshiya Tsutji; Rachel Henkens; Changjun Zhu; Christine Louis-dit-Sully; Michel Moutschen; Wei Jiang; Tomas Mustelin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2006-04-09
Journal Detail:
Title:  Nature cell biology     Volume:  8     ISSN:  1465-7392     ISO Abbreviation:  Nat. Cell Biol.     Publication Date:  2006 May 
Date Detail:
Created Date:  2006-05-12     Completed Date:  2006-06-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100890575     Medline TA:  Nat Cell Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  524-31     Citation Subset:  IM    
Affiliation:
The Burnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
COS Cells
Cell Aging / physiology*
Cell Division / physiology*
Cells, Cultured
Cercopithecus aethiops
DNA / biosynthesis
Dual Specificity Phosphatase 3
Extracellular Signal-Regulated MAP Kinases / metabolism
Hela Cells
Humans
JNK Mitogen-Activated Protein Kinases / metabolism
MAP Kinase Kinase Kinases / metabolism
Protein Tyrosine Phosphatases / deficiency*,  genetics,  metabolism*
RNA, Small Interfering / genetics
S Phase / physiology*
Grant Support
ID/Acronym/Agency:
AI35603/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/RNA, Small Interfering; 9007-49-2/DNA; EC 2.7.11.24/Extracellular Signal-Regulated MAP Kinases; EC 2.7.11.24/JNK Mitogen-Activated Protein Kinases; EC 2.7.11.25/MAP Kinase Kinase Kinases; EC 3.1.3.48/DUSP3 protein, human; EC 3.1.3.48/Dual Specificity Phosphatase 3; EC 3.1.3.48/Protein Tyrosine Phosphatases
Comments/Corrections
Erratum In:
Nat Cell Biol. 2006 Jun;8(6):642

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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