期刊
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 26
卷 26, 期 -, 页码 397-419出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-cellbio-100109-104020
关键词
integrins; conformational change; insolubility; fibrillar; type I collagen; microfibrils
资金
- NIGMS NIH HHS [T32GM007388, T32 GM007388] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007388] Funding Source: NIH RePORTER
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 alpha 5 beta 1 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.
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