Fibronectins, their fibrillogenesis, and in vivo functions

Jean E. Schwarzbauer, Douglas W. DeSimone

Research output: Contribution to journalReview article

204 Scopus citations

Abstract

Fibronectin (FN) is a multidomain protein with the ability to bind simultaneously to cell surface receptors, collagen, proteoglycans, and other FN molecules. Many of these domains and interactions are also involved in the assembly of FN dimers into a multimeric fibrillar matrix. When, where, and how FN binds to its various partners must be controlled and coordinated during fibrillogenesis. Steps in the process of FN fibrillogenesis including FN self-association, receptor activities, and intracellular pathways have been under intense investigation for years. In this review, the domain organization of FN including the extra domains and variable region that are controlled by alternative splicing are described. We discuss how FN-FN and cell-FN interactions play essential roles in the initiation and progression of matrix assembly using complementary results from cell culture and embryonic model systems that have enhanced our understanding of this process.

Original languageEnglish (US)
Pages (from-to)1-19
Number of pages19
JournalCold Spring Harbor Perspectives in Biology
Volume3
Issue number7
DOIs
StatePublished - Jul 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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