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Publication : Band 4.1 proteins regulate integrin-dependent cell spreading.

First Author  Jung Y Year  2012
Journal  Biochem Biophys Res Commun Volume  426
Issue  4 Pages  578-84
PubMed ID  22982319 Mgi Jnum  J:190121
Mgi Id  MGI:5448099 Doi  10.1016/j.bbrc.2012.08.129
Citation  Jung Y, et al. (2012) Band 4.1 proteins regulate integrin-dependent cell spreading. Biochem Biophys Res Commun 426(4):578-84
abstractText  Integrins link the extracellular matrix (ECM) to the cytoskeleton to control cell behaviors including adhesion, spreading and migration. Band 4.1 proteins contain 4.1, ezrin, radixin, moesin (FERM) domains that likely mediate signaling events and cytoskeletal reorganization via integrins. However, the mechanisms by which Band 4.1 proteins and integrins are functionally interconnected remain enigmatic. Here we have investigated roles for Band 4.1 proteins in integrin-mediated cell spreading using primary astrocytes as a model system. We demonstrate that Proteins 4.1B and 4.1G show dynamic patterns of sub-cellular localization in astrocytes spreading on fibronectin. During early stages of cell spreading Proteins 4.1B and 4.1G are enriched in ECM adhesion sites but become more diffusely localized at later stages of spreading. Combinatorial inactivation of Protein 4.1B and 4.1G expression leads to impaired astrocyte spreading. Furthermore, in exogenous expression systems we show that the isolated Protein 4.1 FERM domain significantly enhances integrin-mediated cell spreading. Protein 4.1B is dispensable for reactive astrogliosis in experimental models of cortical injury, likely due to functional compensation by related Protein 4.1 family members. Collectively, these findings reveal that Band 4.1 proteins are important intracellular components for integrin-mediated cell spreading.
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