Goodpasture antigen-binding protein (GPBP) directs myofibril formation: identification of intracellular downstream effector 130-kDa GPBP-interacting protein (GIP130).

Revert-Ros F, López-Pascual E, Granero-Moltó F, Macías J, Breyer R, Zent R, Hudson BG, Saadeddin A, Revert F, Blasco R, Navarro C, Burks D, Saus J
J Biol Chem. 2011 286 (40): 35030-43

PMID: 21832087 · PMCID: PMC3186396 · DOI:10.1074/jbc.M111.249458

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.

MeSH Terms (19)

Animals Basement Membrane Blood Proteins Carrier Proteins Cell Line Collagen DNA-Binding Proteins Gene Expression Regulation Intracellular Signaling Peptides and Proteins Male Mice Mice, Inbred C57BL Mice, Knockout Mice, Transgenic Myoblasts Myofibrils Phosphorylation Protein-Serine-Threonine Kinases Recombinant Proteins

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