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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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Abstract:
Fibronectin (FN) extracellular matrix contributes to multiple cellular processes as an adhesive framework and a source of environmental signals. FN functions primarily from within a fibrillar network. Its assembly into fibrils is mediated by interactions with integrin receptors and is facilitated by sulfation of the syndecan-2 receptor. Receptor binding induces domain-specific conformational changes that promote assembly. Fluorescence resonance energy transfer (FRET) analyses show that III1-2, a domain that is essential for formation of stable detergent-insoluble fibrils, undergoes conformational changes that stimulate FN-FN interactions. Additional regions of FN that enhance fibril stability are being identified using proteomic analysis of detergent-insoluble fibrils. Assembled FN matrix supports cell movements in development and disease. Cell interactions with FN matrix are modulated by the presence of other matrix proteins (such as tenascin-C and fibulin-1), by mechanical forces, and by changes in FN expression or deposition. For example, embryonic stem (ES) cells require adhesion to intermediate levels of FN matrix in order to undergo self-renewal. Knockdown of FN expression in ES cells or increased levels of FN substrate induce ES cell differentiation. Thus, the balance of cell-FN interactions plays important roles in FN fibril assembly and in controlling cell signaling and cell fate decisions.
Faculty Host: Thom Barker, 404.385.5039
