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Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function.
Barzik, Melanie; McClain, Leslie M; Gupton, Stephanie L; Gertler, Frank B.
Afiliação
  • Barzik M; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139 melanie.barzik@nih.gov.
  • McClain LM; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139.
  • Gupton SL; Department of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
  • Gertler FB; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139.
Mol Biol Cell ; 25(17): 2604-19, 2014 Sep 01.
Article em En | MEDLINE | ID: mdl-24989797
Filopodia are long plasma membrane extensions involved in the formation of adhesive, contractile, and protrusive actin-based structures in spreading and migrating cells. Whether filopodia formed by different molecular mechanisms equally support these cellular functions is unresolved. We used Enabled/vasodilator-stimulated phosphoprotein (Ena/VASP)-deficient MV(D7) fibroblasts, which are also devoid of endogenous mDia2, as a model system to investigate how these different actin regulatory proteins affect filopodia morphology and dynamics independently of one another. Filopodia initiated by either Ena/VASP or mDia2 contained similar molecular inventory but differed significantly in parameters such as number, length, F-actin organization, lifetime, and protrusive persistence. Moreover, in the absence of Ena/VASP, filopodia generated by mDia2 did not support initiation of integrin-dependent signaling cascades required for adhesion and subsequent lamellipodial extension, thereby causing a defect in early cell spreading. Coexpression of VASP with constitutively active mDia2(M/A) rescued these early adhesion defects. We conclude that Ena/VASP and mDia2 support the formation of filopodia with significantly distinct properties and that Ena/VASP regulates mDia2-initiated filopodial morphology, dynamics, and function.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfoproteínas / Pseudópodes / Moléculas de Adesão Celular / Proteínas do Citoesqueleto / Proteínas dos Microfilamentos / Proteínas Associadas aos Microtúbulos / NADPH Desidrogenase Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfoproteínas / Pseudópodes / Moléculas de Adesão Celular / Proteínas do Citoesqueleto / Proteínas dos Microfilamentos / Proteínas Associadas aos Microtúbulos / NADPH Desidrogenase Idioma: En Ano de publicação: 2014 Tipo de documento: Article