The ins and outs of fibronectin matrix assembly

Iwona Wierzbicka-Patynowski, Jean E. Schwarzbauer

Research output: Contribution to journalReview article

361 Scopus citations

Abstract

Cell phenotype is specified by environmental cues embedded in the architecture and composition of the extracellular matrix (ECM). Much has been learned about matrix organization and assembly through analyses of the ECM protein fibronectin (FN). FN matrix assembly is a cell-mediated process in which soluble dimeric FN is converted into a fibrillar network. Binding of cell surface integrin receptors to FN converts it to an active form, which promotes fibril formation through interactions with other cell-associated FN dimers. As FN fibrils form on the outside of the cell, cytoplasmic domains of integrin receptors organize cytoplasmic proteins into functional complexes inside. Intracellular connections to the actin cytoskeletal network and stimulation of certain key intracellular signaling pathways are essential for FN-integrin interactions and propagation of FN fibril formation. Thus, assembly of native functional ECM depends on exquisite coordination between extracellular events and intracellular pathways.

Original languageEnglish (US)
Pages (from-to)3269-3276
Number of pages8
JournalJournal of cell science
Volume116
Issue number16
DOIs
StatePublished - Aug 15 2003

All Science Journal Classification (ASJC) codes

  • Cell Biology

Keywords

  • Extracellular matrix
  • Fibril
  • Fibronectin
  • Integrin
  • Intracellular signalling
  • Receptor

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