| Vimentin organization modulates the formation of lamellipodia. | |
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MedLine Citation:
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PMID: 21346197 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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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:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-02-23 |
Journal Detail:
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Title: Molecular biology of the cell Volume: 22 ISSN: 1939-4586 ISO Abbreviation: Mol. Biol. Cell Publication Date: 2011 Apr |
Date Detail:
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Created Date: 2011-04-18 Completed Date: 2011-08-16 Revised Date: 2011-08-19 |
Medline Journal Info:
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Nlm Unique ID: 9201390 Medline TA: Mol Biol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 1274-89 Citation Subset: IM |
Affiliation:
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Department of Urology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Movement* Cell Polarity Escherichia coli Gene Expression Gene Silencing Humans Intermediate Filaments / metabolism Mice Mice, Knockout Microinjections NIH 3T3 Cells Neuropeptides / genetics, metabolism* Peptide Fragments / genetics, metabolism* Phosphorylation 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* |
| Grant Support | |
ID/Acronym/Agency:
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GM-036806/GM/NIGMS NIH HHS; GM-057464/GM/NIGMS NIH HHS; NS-071216/NS/NINDS NIH HHS; R01 GM057464-11/GM/NIGMS NIH HHS; R01 GM057464-12/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Neuropeptides; 0/Peptide Fragments; 0/RNA, Small Interfering; 0/Rac1 protein, mouse; 0/Recombinant Fusion Proteins; 0/Vimentin; 56-45-1/Serine; EC 2.7.11.1/p21-Activated Kinases; EC 3.6.5.2/rac GTP-Binding Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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