Assembly of fibronectin extracellular matrix

Purva Singh, Cara Carraher, Jean E. Schwarzbauer

Research output: Contribution to journalReview article

454 Scopus citations

Abstract

In the process of matrix assembly, multivalent extracellular matrix (ECM) proteins are induced to self-associate and to interact with other ECM proteins to form fibrillar networks. Matrix assembly is usually initiated by ECM glycoproteins binding to cell surface receptors, such as fibronectin (FN) dimers binding to α5β1 integrin. Receptor binding stimulates FN self-association mediated by the N-terminal assembly domain and organizes the actin cytoskeleton to promote cell contractility. FN conformational changes expose additional binding sites that participate in fibril formation and in conversion of fibrils into a stabilized, insoluble form. Once assembled, the FN matrix impacts tissue organization by contributing to the assembly of other ECM proteins. Here, we describe the major steps, molecular interactions, and cellular mechanisms involved in assembling FN dimers into fibrillar matrix while highlighting important issues and major questions that require further investigation.

Original languageEnglish (US)
Pages (from-to)397-419
Number of pages23
JournalAnnual review of cell and developmental biology
Volume26
DOIs
StatePublished - Nov 10 2010

All Science Journal Classification (ASJC) codes

  • Developmental Biology
  • Cell Biology

Keywords

  • conformational change
  • fibrillar
  • insolubility
  • integrins
  • microfibrils
  • type I collagen

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