title: Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins.
abstract: By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and alpha-actinin and colocalizes with vinculin/metavinculin and alpha-actinin at microfilament attachment sites, such as cell-cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH2-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites.
authors.affiliation: Cell Biology, Zoological Institute, Technical University of Braunschweig, D-38092 Braunschweig, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Hüttelmaier
authors.forename: S
authors.initials: S
authors.lastname: Illenberger
authors.forename: I
authors.initials: I
authors.lastname: Grosheva
authors.forename: M
authors.initials: M
authors.lastname: Rüdiger
authors.forename: R H
authors.initials: RH
authors.lastname: Singer
authors.forename: B M
authors.initials: BM
authors.lastname: Jockusch
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000185:Actinin / Q000378:metabolism*; D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004847:Epithelial Cells / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D007365:Intercellular Junctions / Q000378:metabolism; D008024:Ligands; D051379:Mice; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000166:cytology / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D038941:Polypyrimidine Tract-Binding Protein; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012261:Ribonucleoproteins / Q000235:genetics / Q000378:metabolism*; D014018:Tissue Distribution; D020798:Two-Hybrid System Techniques; D016596:Vinculin / Q000031:analogs & derivatives / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D008024:Ligands; D009687:Nuclear Proteins; C486705:RAVER1 protein, human; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; C442838:Raver1 protein, mouse; D011993:Recombinant Fusion Proteins; D012261:Ribonucleoproteins; D000185:Actinin; D016596:Vinculin; D038941:Polypyrimidine Tract-Binding Protein