@article{83566,
  keywords = {Protein Structure, Tertiary, solubility, Models, Biological, Embryo, Mammalian, Fibronectins, Extracellular Matrix, Alternative Splicing, Protein Interaction Domains and Motifs, Protein Isoforms, Protein Stability},
  author = {Jean Schwarzbauer and Douglas DeSimone},
  title = {Fibronectins, their fibrillogenesis, and in vivo functions.},
  abstract = {<p>Fibronectin (FN) is a multidomain protein with the ability to bind simultaneously to cell surface receptors, collagen, proteoglycans, and other FN molecules. Many of these domains and interactions are also involved in the assembly of FN dimers into a multimeric fibrillar matrix. When, where, and how FN binds to its various partners must be controlled and coordinated during fibrillogenesis. Steps in the process of FN fibrillogenesis including FN self-association, receptor activities, and intracellular pathways have been under intense investigation for years. In this review, the domain organization of FN including the extra domains and variable region that are controlled by alternative splicing are described. We discuss how FN-FN and cell-FN interactions play essential roles in the initiation and progression of matrix assembly using complementary results from cell culture and embryonic model systems that have enhanced our understanding of this process.</p>
},
  year = {2011},
  journal = {Cold Spring Harb Perspect Biol},
  volume = {3},
  month = {07/2011},
  issn = {1943-0264},
  doi = {10.1101/cshperspect.a005041},
  language = {eng},
}