title: Close encounters: regulation of vertebrate skeletal myogenesis by cell-cell contact.
abstract: Cells of the vertebrate skeletal muscle lineage develop in a highly ordered process that includes specification, migration and differentiation into multinucleated myofibers. The changes in gene expression and cell morphology that occur during myogenic differentiation must be coordinated with each other in a spatiotemporal fashion; one way that this might occur is through regulation of these processes by cell-cell adhesion and resultant signaling. The past several years have witnessed the identification of molecules that are likely to be mediators of the promyogenic effects of cell-cell contact and some of the mechanisms by which they work. These include: the community factor, embryonic fibroblast growth factor (eFGF); classical cadherins, which mediate both adhesion and signaling; and cadherin-associated immunoglobulin superfamily members such as CDO, BOC and neogenin. Genetic evidence for the promyogenic roles of some of these factors is emerging. In other cases, potential compensatory or redundant functions necessitate future construction of double or triple mutants. Mechanistic studies in vitro indicate that specific cadherins and immunoglobulin superfamily proteins exert some of their effects in an interdependent fashion by signaling from a multiprotein complex found at sites of cell-cell contact.
authors.affiliation: Brookdale Department of Molecular, Cell and Developmental Biology, Mount Sinai School of Medicine, New York, NY 10029, USA. robert.krauss@mssm.edu
authors.forename: Robert S
authors.initials: RS
authors.lastname: Krauss
authors.forename: Francesca
authors.initials: F
authors.lastname: Cole
authors.forename: Ursula
authors.initials: U
authors.lastname: Gaio
authors.forename: Giichi
authors.initials: G
authors.lastname: Takaesu
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Jong-Sun
authors.initials: JS
authors.lastname: Kang
mesh_terms: D000818:Animals; D015820:Cadherins / Q000096:biosynthesis / Q000235:genetics; D002448:Cell Adhesion / Q000235:genetics / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism; D002450:Cell Communication; D002454:Cell Differentiation / Q000235:genetics / Q000502:physiology*; D002465:Cell Movement / Q000235:genetics / Q000502:physiology; D005346:Fibroblast Growth Factors / Q000096:biosynthesis / Q000235:genetics; D018507:Gene Expression Regulation, Developmental / Q000235:genetics / Q000502:physiology*; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D024510:Muscle Development / Q000235:genetics / Q000502:physiology*; D010446:Peptide Fragments / Q000096:biosynthesis / Q000235:genetics; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology; D025521:Tumor Suppressor Proteins / Q000235:genetics / Q000378:metabolism; D014714:Vertebrates
chemical_list: C474334:BOC protein, human; C107286:CDON protein, human; D015820:Cadherins; D015815:Cell Adhesion Molecules; C502403:FAT1 protein, human; D007074:Immunoglobulin G; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D025521:Tumor Suppressor Proteins; C091279:neogenin; D005346:Fibroblast Growth Factors; C052888:fibroblast growth factor (1-10)