| The cofilin activity cycle in lamellipodia and invadopodia. | |
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MedLine Citation:
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PMID: 19862699 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The actin severing protein cofilin is essential for directed cell migration and chemotaxis, in many cell types and is also important for tumor cell invasion during metastasis. Through its severing activity, cofilin increases the number of free barbed ends to initiate actin polymerization for actin-based protrusion in two distinct subcellular compartments in invasive tumor cells: lamellipodia and invadopodia. Cofilin severing activity is tightly regulated and multiple mechanisms are utilized to regulate cofilin activity. In this prospect, we have grouped the primary on/off regulation into two broad categories, both of which are important for inhibiting cofilin from binding to F-actin or G-actin: (1) Blocking cofilin activity by the binding of cofilin to either PI(4,5)P(2) at lamellipodia, or cortactin at invadopodia. (2) Blocking cofilin's ability to bind to actin via serine phosphorylation. Although the literature suggests that these cofilin regulatory mechanisms may be cell-type dependent, we propose the existence of a common cofilin activity cycle in which both operate. In this common cycle, the mechanism used to initiate cofilin activity is determined by the starting point in the cycle in a given subcellular compartment. |
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Authors:
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Matthew Oser; John Condeelis |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Review |
Journal Detail:
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Title: Journal of cellular biochemistry Volume: 108 ISSN: 1097-4644 ISO Abbreviation: J. Cell. Biochem. Publication Date: 2009 Dec |
Date Detail:
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Created Date: 2009-12-01 Completed Date: 2010-03-11 Revised Date: 2010-12-17 |
Medline Journal Info:
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Nlm Unique ID: 8205768 Medline TA: J Cell Biochem Country: United States |
Other Details:
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Languages: eng Pagination: 1252-62 Citation Subset: IM |
Copyright Information:
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(c) 2009 Wiley-Liss, Inc. |
Affiliation:
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Department of Anatomy and Structural Biology, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461, USA. moser@aecom.yu.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actin Depolymerizing Factors
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metabolism* Actins / metabolism Animals Cell Movement Humans Phosphorylation Pseudopodia / metabolism* Serine / genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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CA100324/CA/NCI NIH HHS; CA126511/CA/NCI NIH HHS; GM064346/GM/NIGMS NIH HHS; GM38511/GM/NIGMS NIH HHS; P01 CA100324-01/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Actin Depolymerizing Factors; 0/Actins; 56-45-1/Serine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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