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Roles of myosin-V in integrin recycling and focal adhesion dynamics

Grant number: 12/24983-0
Support Opportunities:Scholarships abroad - Research Internship - Doctorate
Effective date (Start): April 12, 2013
Effective date (End): February 11, 2014
Field of knowledge:Biological Sciences - Biology
Principal Investigator:Enilza Maria Espreafico
Grantee:Anelisa Ramão
Supervisor: Gregg G. Gundersen
Host Institution: Faculdade de Medicina de Ribeirão Preto (FMRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Research place: Columbia University in the City of New York, United States  
Associated to the scholarship:10/01197-4 - Myosin-Va promotes focal adhesion disassembly and cell migration, BP.DR


Focal adhesion turnover is crucial for cell migration. Through this process, focal complexes disassemble and their components reassemble into new focal contacts. Focal adhesion disassembly occurs through clathrin-dependent endocytosis of integrin and also requires microtubule and FAK. Endocytosed integrins entering early endosomal vesicles (Rab5) end up eventually to late endosomes, but most frequently to recycling compartments to be delivered to the plasma membrane to assemble new focal contacts. Unpublished data from Dr. Gregg Gundersen group (Columbia University - NY) show that focal adhesion reassembly, after microtubule-induced disassembly, occurs upon integrin recycling, which is dependent of Rab11 and active forms of FAK and Src. Results from our laboratory show that myosin-Va interacts with FAK and influences its localization and activation and appears to be required for microtubule-induced focal adhesion disassembly. Also, we observed that knock-down of myosin-Va in melanoma cells results in deficient cell adhesion to different types of extracellular matrix concomitant with reduced ²1-integrin expression on the cell surface. The existing link among myosin-V and Rabs and our data connecting myosin-Va to focal adhesion dynamics lead to questions of how myosin-Va would influence integrin recycling and the importance of its interaction with FAK in this process. Therefore, this project aims at assessing the role of myosin-Va and its interaction with FAK in focal adhesion disassembly, integrin recycling and the reassembly of new focal contacts. These objectives are supported by our current data and fit perfectly with the ongoing projects from Dr. Gundersen's laboratory. Finally, we ask if the three members of class V myosins act in a redundant or cooperative way and if they are differentially needed in distinct type of cells or after oncogenic transformation. These issues are of fundamental importance to understand the key mechanisms of cell migration and for the development of new therapeutic strategies. (AU)

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