Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins

Stefan Hüttelmaier, Susanne Illenberger, Irina Grosheva, Manfred Rüdiger, Robert H. Singer, Brigitte M. Jockusch

Research output: Contribution to journalArticlepeer-review

95 Scopus citations


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 micro filament-associated proteins vinculin, metavinculin, and α-actinin and colocalizes with vinculin/metavinculin and α-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.

Original languageEnglish (US)
Pages (from-to)775-785
Number of pages11
JournalJournal of Cell Biology
Issue number5
StatePublished - Nov 26 2001


  • Microfilament attachment
  • PTB/hnRNPI
  • Vinculin/Metavinculin
  • hnRNP
  • α-actinin

ASJC Scopus subject areas

  • Cell Biology


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