Document Detail


Nir2, a novel regulator of cell morphogenesis.
MedLine Citation:
PMID:  11909959     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell morphogenesis requires dynamic reorganization of the actin cytoskeleton, a process that is tightly regulated by the Rho family of small GTPases. These GTPases act as molecular switches by shuttling between their inactive GDP-bound and active GTP-bound forms. Here we show that Nir2, a novel protein related to Drosophila retinal degeneration B (RdgB), markedly affects cell morphology through a novel Rho-inhibitory domain (Rid) which resides in its N-terminal region. Rid exhibits sequence homology with the Rho-binding site of formin-homology (FH) proteins and leads to an apparent loss of F-actin staining when ectopically expressed in mammalian cells. We also show that Rid inhibits Rho-mediated stress fiber formation and lysophosphatidic acid-induced RhoA activation. Biochemical studies demonstrated that Nir2, via Rid, preferentially binds to the inactive GDP-bound form of the small GTPase Rho. Microinjection of antibodies against Nir2 into neuronal cells markedly attenuates neurite extension, whereas overexpression of Nir2 in these cells attenuates Rho-mediated neurite retraction. These results implicate Nir2 as a novel regulator of the small GTPase Rho in actin cytoskeleton reorganization and cell morphogenesis.
Authors:
Donghua Tian; Vladimir Litvak; Maria Toledo-Rodriguez; Shari Carmon; Sima Lev
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  22     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-03-22     Completed Date:  2002-04-22     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2650-62     Citation Subset:  IM    
Affiliation:
Department of Neurobiology, Weizmann Institute of Science, Rehovot 76100, Israel.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Actins / metabolism
Amino Acid Sequence
Animals
Binding Sites
COS Cells
Calcium-Binding Proteins / chemistry,  genetics,  physiology*
Cell Differentiation / genetics,  physiology*
Cell Line
Cytoskeleton / metabolism
Eye Proteins*
Hela Cells
Humans
Membrane Proteins*
Mice
Molecular Sequence Data
Neurons / cytology,  metabolism
Protein Structure, Tertiary
Recombinant Proteins / chemistry,  genetics,  metabolism
Sequence Deletion
Sequence Homology, Amino Acid
rho GTP-Binding Proteins / metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Calcium-Binding Proteins; 0/Eye Proteins; 0/Membrane Proteins; 0/PITPNM1 protein, human; 0/Pitpnm protein, mouse; 0/Recombinant Proteins; EC 3.6.5.2/rho GTP-Binding Proteins
Comments/Corrections

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


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