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• W2034734211 abstract "Fibronectin (FN) assembly into extracellular matrix is tightly regulated and essential to embryogenesis and wound healing. FN fibrillogenesis is initiated by cytoskeleton-derived tensional forces transmitted across transmembrane integrins onto RGD binding sequences within the tenth FN type III (10FNIII) domains. These forces unfold 10FNIII to expose cryptic FN assembly sites; however, a specific sequence has not been identified in 10FNIII. Our past steered molecular dynamics simulations modeling 10FNIII unfolding by force at its RGD loop predicted a mechanical intermediate with a solvent-exposed N terminus spanning the A and B β-strands. Here, we experimentally confirm that the predicted 23-residue cryptic peptide 1 (CP1) initiates FN multimerization, which is mediated by interactions with 10FNIII that expose hydrophobic surfaces that support 8-anilino-1-napthalenesulfonic acid binding. Localization of multimerization activity to the C terminus led to the discovery of a minimal 7-amino acid “multimerization sequence” (SLLISWD), which induces polymerization of FN and the clotting protein fibrinogen in addition to enhancing FN fibrillogenesis in fibroblasts. A point mutation at Trp-6 that reduces exposure of hydrophobic sites for 8-anilino-1-napthalenesulfonic acid binding and β-structure formation inhibits FN multimerization and prevents physiological cell-based FN assembly in culture. We propose a model for cell-mediated fibrillogenesis whereby cell traction force initiates a cascade of intermolecular exchange starting with the unfolding of 10FNIII to expose the multimerization sequence, which interacts with strand B of another 10FNIII domain via a Trp-mediated β-strand exchange to stabilize a partially unfolded intermediate that propagates FN self-assembly.Background: Fibronectin matrix assembly is mediated by cell traction at the RGD loop of 10FNIII, which is predicted to unravel β-strands A and B.Results: Sequence SLLISWD from strand B initiates fibronectin multimerization.Conclusion: SLLISWD mediates cell-mediated fibronectin fibril assembly.Significance: This matrix motif provides insight into physiological fibronectin fibrillogenesis with utility in initiating matrix assembly for tissue repair. Fibronectin (FN) assembly into extracellular matrix is tightly regulated and essential to embryogenesis and wound healing. FN fibrillogenesis is initiated by cytoskeleton-derived tensional forces transmitted across transmembrane integrins onto RGD binding sequences within the tenth FN type III (10FNIII) domains. These forces unfold 10FNIII to expose cryptic FN assembly sites; however, a specific sequence has not been identified in 10FNIII. Our past steered molecular dynamics simulations modeling 10FNIII unfolding by force at its RGD loop predicted a mechanical intermediate with a solvent-exposed N terminus spanning the A and B β-strands. Here, we experimentally confirm that the predicted 23-residue cryptic peptide 1 (CP1) initiates FN multimerization, which is mediated by interactions with 10FNIII that expose hydrophobic surfaces that support 8-anilino-1-napthalenesulfonic acid binding. Localization of multimerization activity to the C terminus led to the discovery of a minimal 7-amino acid “multimerization sequence” (SLLISWD), which induces polymerization of FN and the clotting protein fibrinogen in addition to enhancing FN fibrillogenesis in fibroblasts. A point mutation at Trp-6 that reduces exposure of hydrophobic sites for 8-anilino-1-napthalenesulfonic acid binding and β-structure formation inhibits FN multimerization and prevents physiological cell-based FN assembly in culture. We propose a model for cell-mediated fibrillogenesis whereby cell traction force initiates a cascade of intermolecular exchange starting with the unfolding of 10FNIII to expose the multimerization sequence, which interacts with strand B of another 10FNIII domain via a Trp-mediated β-strand exchange to stabilize a partially unfolded intermediate that propagates FN self-assembly. Background: Fibronectin matrix assembly is mediated by cell traction at the RGD loop of 10FNIII, which is predicted to unravel β-strands A and B. Results: Sequence SLLISWD from strand B initiates fibronectin multimerization. Conclusion: SLLISWD mediates cell-mediated fibronectin fibril assembly. Significance: This matrix motif provides insight into physiological fibronectin fibrillogenesis with utility in initiating matrix assembly for tissue repair." @default.
• W2034734211 created "2016-06-24" @default.
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• W2034734211 date "2013-07-01" @default.
• W2034734211 modified "2023-10-18" @default.
• W2034734211 title "SLLISWD Sequence in the 10FNIII Domain Initiates Fibronectin Fibrillogenesis" @default.
• W2034734211 cites W1026183415 @default.
• W2034734211 cites W149720224 @default.
• W2034734211 cites W1504989678 @default.
• W2034734211 cites W1521958691 @default.
• W2034734211 cites W1534818109 @default.
• W2034734211 cites W1550344038 @default.
• W2034734211 cites W1568633684 @default.
• W2034734211 cites W1586370846 @default.
• W2034734211 cites W1590619267 @default.
• W2034734211 cites W1598194406 @default.
• W2034734211 cites W1963631969 @default.
• W2034734211 cites W1964895264 @default.
• W2034734211 cites W1971679287 @default.
• W2034734211 cites W1976140150 @default.
• W2034734211 cites W1978150593 @default.
• W2034734211 cites W1980364322 @default.
• W2034734211 cites W1982137055 @default.
• W2034734211 cites W1991210194 @default.
• W2034734211 cites W1996734830 @default.
• W2034734211 cites W1996913210 @default.
• W2034734211 cites W2000829418 @default.
• W2034734211 cites W2001103206 @default.
• W2034734211 cites W2003473363 @default.
• W2034734211 cites W2003997440 @default.
• W2034734211 cites W2012998128 @default.
• W2034734211 cites W2020388963 @default.
• W2034734211 cites W2020645507 @default.
• W2034734211 cites W2023692836 @default.
• W2034734211 cites W2023989365 @default.
• W2034734211 cites W2024895368 @default.
• W2034734211 cites W2029003138 @default.
• W2034734211 cites W2037318971 @default.
• W2034734211 cites W2038399240 @default.
• W2034734211 cites W2045032642 @default.
• W2034734211 cites W2048138119 @default.
• W2034734211 cites W2049280483 @default.
• W2034734211 cites W2053942176 @default.
• W2034734211 cites W2062278312 @default.
• W2034734211 cites W2064297038 @default.
• W2034734211 cites W2065799167 @default.
• W2034734211 cites W2069478980 @default.
• W2034734211 cites W2072320843 @default.
• W2034734211 cites W2073079122 @default.
• W2034734211 cites W2073466675 @default.
• W2034734211 cites W2092597250 @default.
• W2034734211 cites W2092730327 @default.
• W2034734211 cites W2101712645 @default.
• W2034734211 cites W2104017463 @default.
• W2034734211 cites W2104876248 @default.
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• W2034734211 cites W2108050451 @default.
• W2034734211 cites W2109088595 @default.
• W2034734211 cites W2120383690 @default.
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• W2034734211 cites W2139117025 @default.
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• W2034734211 cites W2159066422 @default.
• W2034734211 cites W2163187600 @default.
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• W2034734211 doi "https://doi.org/10.1074/jbc.m113.462077" @default.
• W2034734211 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3774401" @default.
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