Document Detail


RhoG regulates anoikis through a phosphatidylinositol 3-kinase-dependent mechanism.
MedLine Citation:
PMID:  17570359     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In normal epithelial cells, cell-matrix interaction is required for cell survival and proliferation, whereas disruption of this interaction causes epithelial cells to undergo apoptosis called anoikis. Here we show that the small GTPase RhoG plays an important role in the regulation of anoikis. HeLa cells are capable of anchorage-independent cell growth and acquire resistance to anoikis. We found that RNA interference-mediated knockdown of RhoG promoted anoikis in HeLa cells. Previous studies have shown that RhoG activates Rac1 and induces several cellular functions including promotion of cell migration through its effector ELMO and the ELMO-binding protein Dock180 that function as a Rac-specific guanine nucleotide exchange factor. However, RhoG-induced suppression of anoikis was independent of the ELMO- and Dock180-mediated activation of Rac1. On the other hand, the regulation of anoikis by RhoG required phosphatidylinositol 3-kinase (PI3K) activity, and constitutively active RhoG bound to the PI3K regulatory subunit p85alpha and induced the PI3K-dependent phosphorylation of Akt. Taken together, these results suggest that RhoG protects cells from apoptosis caused by the loss of anchorage through a PI3K-dependent mechanism, independent of its activation of Rac1.
Authors:
Nao Yamaki; Manabu Negishi; Hironori Katoh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-05-18
Journal Detail:
Title:  Experimental cell research     Volume:  313     ISSN:  0014-4827     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-08-06     Completed Date:  2007-09-19     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2821-32     Citation Subset:  IM    
Affiliation:
Laboratory of Molecular Neurobiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / antagonists & inhibitors,  metabolism*
Adaptor Proteins, Signal Transducing / metabolism
Amino Acid Sequence
Animals
Anoikis* / genetics
Base Sequence
Cell Movement
Chromones / pharmacology
Hela Cells
Humans
Mice
Molecular Sequence Data
Morpholines / pharmacology
Phosphorylation
Proto-Oncogene Proteins c-akt / metabolism
RNA Interference
RNA, Small Interfering / pharmacology
rac GTP-Binding Proteins / metabolism
rac1 GTP-Binding Protein / metabolism
rho GTP-Binding Proteins / antagonists & inhibitors,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Chromones; 0/DOCK1 protein, human; 0/ELMO1 protein, human; 0/Morpholines; 0/RNA, Small Interfering; 147605-13-8/RHOG protein, human; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.6.5.2/rac GTP-Binding Proteins; EC 3.6.5.2/rac1 GTP-Binding Protein; EC 3.6.5.2/rho GTP-Binding Proteins

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


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