Document Detail


A big new job for small GTPases.
MedLine Citation:
PMID:  22647313     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Members of the Ras superfamily of small guanosine triphosphatases (GTPases) function as key nodes within signaling networks in a remarkable range of cellular processes, including cell proliferation, differentiation, growth, cell-cell adhesion and apoptosis. We recently described a novel role for the Ras-like small GTPases Rap1 and Ral in regulating cortical polarity and spindle orientation during asymmetric neuroblast division in Drosophila. The participation of these proteins in promoting cell polarization seems to be a common theme throughout evolution.
Authors:
Ana Carmena
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-05-31
Journal Detail:
Title:  Small GTPases     Volume:  3     ISSN:  2154-1256     ISO Abbreviation:  Small GTPases     Publication Date:    2012 Jul-Sep
Date Detail:
Created Date:  2012-08-29     Completed Date:  2013-04-03     Revised Date:  2013-07-02    
Medline Journal Info:
Nlm Unique ID:  101530974     Medline TA:  Small GTPases     Country:  United States    
Other Details:
Languages:  eng     Pagination:  159-62     Citation Subset:  IM    
Affiliation:
Instituto de Neurociencias, CSIC/UMH, 03550-Sant Joan d'Alacant, Alicante, Spain. acarmena@umh.es
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Polarity
Drosophila / cytology,  metabolism
Drosophila Proteins / metabolism
Humans
Monomeric GTP-Binding Proteins / metabolism*
Saccharomyces cerevisiae / cytology,  metabolism
Saccharomyces cerevisiae Proteins / metabolism
Signal Transduction
ral GTP-Binding Proteins / metabolism
rap1 GTP-Binding Proteins / metabolism
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/Saccharomyces cerevisiae Proteins; EC 3.6.5.2/Monomeric GTP-Binding Proteins; EC 3.6.5.2/ral GTP-Binding Proteins; EC 3.6.5.2/rap1 GTP-Binding Proteins
Comments/Corrections

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