title: Subunit 3 of the COP9 signalosome is poised to facilitate communication between the extracellular matrix and the nucleus through the muscle-specific beta1D integrin.
abstract: Yeast two-hybrid analysis (Fields and Song, 1989, Nature, 340:245-246) was used to screen a human heart library to isolate proteins interacting with the adult muscle-specific beta1D integrin but not with beta1A integrin. In addition to previously identified interactions (RACK 1(Liliental and Chang, 1998, Journal of Biological Chemistry, 273:2379-2383) and alpha-actinin (Otey et al., 1990, Journal of Cell Biology, 111:721-729), the authors isolated several novel candidates. These include subunit 3 (CSN3/Sgn3) of the COP9 signalosome complex, cyclins D1, D2, and D3, RanBPM, and a recently identified protein COG8/DOR1. These protein interactions were specific for beta1D integrin, as no binding to beta1A integrin cytoplasmic domain was measurable by two-hybrid analysis. This paper presents the initial characterization of the interaction of CSN3 with beta1D integrin, the localization of CSN3 and the other COP9 signalosome subunits in embryonic and adult cardiac myocytes and their response to muscle cell differentiation.
authors.affiliation: University of Utah, Nora Eccles Harrison Cardiovascular Research and Training Institute, Salt Lake City, Utah, USA.
authors.forename: Chris
authors.initials: C
authors.lastname: Hunter
authors.forename: Jennifer
authors.initials: J
authors.lastname: Evans
authors.forename: Maria L
authors.initials: ML
authors.lastname: Valencik
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000818:Animals; D001667:Binding, Competitive; D000075686:COP9 Signalosome Complex; D002450:Cell Communication / Q000502:physiology; D002454:Cell Differentiation / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism*; D049109:Cell Proliferation; D002478:Cells, Cultured; D005109:Extracellular Matrix / Q000378:metabolism*; D006801:Humans; D039641:Integrin beta Chains / Q000378:metabolism*; D019012:Integrin beta1 / Q000378:metabolism*; D051379:Mice; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism; D032446:Myoblasts / Q000166:cytology / Q000378:metabolism; D009206:Myocardium / Q000737:chemistry; D032383:Myocytes, Cardiac / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D011518:Proto-Oncogene Proteins; D015398:Signal Transduction; D020798:Two-Hybrid System Techniques
chemical_list: C000618791:Cops3 protein, mouse; D039641:Integrin beta Chains; D019012:Integrin beta1; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D011518:Proto-Oncogene Proteins; D011494:Protein Kinases; D010447:Peptide Hydrolases; D000075686:COP9 Signalosome Complex