Assembly of Fibronectin Extracellular Matrix

By Purva Singh, C. Carraher, J. Schwarzbauer. Annual Review of Cell and Developmental Biology, 2010

922 citations recorded by the source corpus.

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.

Subfields: Cancer Research, Immunology and Allergy, Oncology

View Paper: https://www.semanticscholar.org/paper/5f57fb431113d8d15b116d385bd0472443d9ef2b

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In Immunology and Allergy

1. E. Mojares
2. Cameron G Walker
3. Armando E. del Río Hernández

Citations in the corpus

• Role of Extracellular Matrix in Development and Cancer Progression (2018, background): “However, this relationship may prove reciprocal as recent studies have also implicated that collagen has a role in enhancing fibronectin assembly [71,84,85].”