Distinct FN modules bind cell surface receptors such as integrins and syndecans () and ECM proteins such as collagens, fibrin, and FN itself ().

Introductionįibronectin (FN) is a ubiquitous and abundant ECM protein, which is secreted as a disulfide-bonded dimer consisting primarily of three types of repeating modules (I, II, and III ). Our findings demonstrate that FN contains a novel motif for integrin binding and fibril formation whose activity is controlled by amino acid modification. Matrix assembly assays and solid-phase binding assays reveal that αvβ3 integrin assembles FN-RGE by binding an isoDGR motif in FN-I 5, which is generated by the nonenzymatic rearrangement of asparagines (N) into an iso-aspartate ( iso-D). Surprisingly, the absence of a functional RGD motif in FN did not compromise assembly of an FN matrix in mutant embryos or on mutant cells. FN-RGE homozygous embryos die at embryonic day 10 with shortened posterior trunk, absent tail bud–derived somites, and severe vascular defects resembling the phenotype of α5 integrin–deficient mice.

To test this hypothesis in vivo, we replaced the RGD motif with the inactive RGE in mice. The interactions of α5β1 or αv integrins with the RGD motif of FN-III repeat 10 (FN-III 10) are considered an essential step in the assembly of FN fibrils. Each subunit contains three types of repeating modules: FN-I, FN-II, and FN-III.

Cher says Broadway show based on her life 'needs work' Pete Davidson thinks Ariana Grande is 'the most precious angel on earth'.Jcellbiol_jcb.200703021_JCB_200703021_FS5-01.jpg (95K) Abstractįibronectin (FN) is secreted as a disulfide-bonded FN dimer.

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