Document Detail

Vimentin organization modulates the formation of lamellipodia.
MedLine Citation:
PMID:  21346197     Owner:  NLM     Status:  MEDLINE    
Vimentin intermediate filaments (VIF) extend throughout the rear and perinuclear regions of migrating fibroblasts, but only nonfilamentous vimentin particles are present in lamellipodial regions. In contrast, VIF networks extend to the entire cell periphery in serum-starved or nonmotile fibroblasts. Upon serum addition or activation of Rac1, VIF are rapidly phosphorylated at Ser-38, a p21-activated kinase phosphorylation site. This phosphorylation of vimentin is coincident with VIF disassembly at and retraction from the cell surface where lamellipodia form. Furthermore, local induction of photoactivatable Rac1 or the microinjection of a vimentin mimetic peptide (2B2) disassemble VIF at sites where lamellipodia subsequently form. When vimentin organization is disrupted by a dominant-negative mutant or by silencing, there is a loss of polarity, as evidenced by the formation of lamellipodia encircling the entire cell, as well as reduced cell motility. These findings demonstrate an antagonistic relationship between VIF and the formation of lamellipodia.
Brian T Helfand; Melissa G Mendez; S N Prasanna Murthy; Dale K Shumaker; Boris Grin; Saleemulla Mahammad; Ueli Aebi; Tatjana Wedig; Yi I Wu; Klaus M Hahn; Masaki Inagaki; Harald Herrmann; Robert D Goldman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-02-23
Journal Detail:
Title:  Molecular biology of the cell     Volume:  22     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-04-18     Completed Date:  2011-08-16     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1274-89     Citation Subset:  IM    
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MeSH Terms
Cell Movement*
Cell Polarity
Escherichia coli
Gene Expression
Gene Silencing
Intermediate Filaments / metabolism
Mice, Knockout
NIH 3T3 Cells
Neuropeptides / genetics,  metabolism*
Peptide Fragments / genetics,  metabolism*
Pseudopodia / genetics,  metabolism*
RNA, Small Interfering / metabolism
Recombinant Fusion Proteins / genetics,  metabolism
Serine / metabolism
Serum / metabolism
Vimentin / genetics,  metabolism*
p21-Activated Kinases / genetics,  metabolism
rac GTP-Binding Proteins / genetics,  metabolism*
rac1 GTP-Binding Protein
Grant Support
Reg. No./Substance:
0/Neuropeptides; 0/Peptide Fragments; 0/RNA, Small Interfering; 0/Rac1 protein, mouse; 0/Recombinant Fusion Proteins; 0/Vimentin; 452VLY9402/Serine; EC Kinases; EC GTP-Binding Proteins; EC GTP-Binding Protein

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