title: Goodpasture antigen-binding protein (GPBP) directs myofibril formation: identification of intracellular downstream effector 130-kDa GPBP-interacting protein (GIP130).
abstract: Goodpasture antigen-binding protein-1 (GPBP-1) is an exportable non-conventional Ser/Thr kinase that regulates glomerular basement membrane collagen organization. Here we provide evidence that GPBP-1 accumulates in the cytoplasm of differentiating mouse myoblasts prior to myosin synthesis. Myoblasts deficient in GPBP-1 display defective myofibril formation, whereas myofibrils assemble with enhanced efficiency in those overexpressing GPBP-1. We also show that GPBP-1 targets the previously unidentified GIP130 (GPBP-interacting protein of 130 kDa), which binds to myosin and promotes its myofibrillar assembly. This report reveals that GPBP-1 directs myofibril formation, an observation that expands its reported role in supramolecular organization of structural proteins to the intracellular compartment.
authors.affiliation: Centro de Investigación Príncipe Felipe, 46012 Valencia, Spain.
authors.forename: Francisco
authors.initials: F
authors.lastname: Revert-Ros
authors.forename: Ernesto
authors.initials: E
authors.lastname: López-Pascual
authors.forename: Froilán
authors.initials: F
authors.lastname: Granero-Moltó
authors.forename: Jesús
authors.initials: J
authors.lastname: Macías
authors.forename: Richard
authors.initials: R
authors.lastname: Breyer
authors.forename: Roy
authors.initials: R
authors.lastname: Zent
authors.forename: Billy G
authors.initials: BG
authors.lastname: Hudson
authors.forename: Anas
authors.initials: A
authors.lastname: Saadeddin
authors.forename: Fernando
authors.initials: F
authors.lastname: Revert
authors.forename: Raül
authors.initials: R
authors.lastname: Blasco
authors.forename: Carmen
authors.initials: C
authors.lastname: Navarro
authors.forename: Deborah
authors.initials: D
authors.lastname: Burks
authors.forename: Juan
authors.initials: J
authors.lastname: Saus
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D003094:Collagen / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005786:Gene Expression Regulation; D047908:Intracellular Signaling Peptides and Proteins; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D008822:Mice, Transgenic; D032446:Myoblasts / Q000378:metabolism; D009210:Myofibrils / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; C504459:FILIP1L protein, human; C568471:GPBP-interacting protein of 130 kDa, mouse; C478882:GPBP1 protein, human; D047908:Intracellular Signaling Peptides and Proteins; D011994:Recombinant Proteins; D003094:Collagen; C568469:Goodpasture antigen-binding protein-1, mouse; D017346:Protein Serine-Threonine Kinases