RNA polymerase II subunit 3 is retained in the cytoplasm by its interaction with HCR, the psoriasis vulgaris candidate gene product

Nicoletta Corbi, Tiziana Bruno, Roberta De Angelis, Monica Di Padova, Valentina Libri, Maria Grazia Di Certo, Laura Spinardi, Aristide Floridi, Maurizio Fanciulli, Claudio Passananti

Research output: Contribution to journalArticlepeer-review

Abstract

Here, we show that the subcellular localization of α-like RNA polymerase II core subunit 3 (RPB3) is regulated during muscle differentiation. We have recently demonstrated that the expression of RPB3 is regulated during muscle differentiation and that, inside RNA polymerase II (RNAP II), it is directly involved in contacting regulatory proteins such as the myogenic transcription factor Myogenin and activating transcription factor ATF4. We show for the first time, that RPB3, in addition to its presence and role inside the RNAP II core enzyme, accumulates in the cytoplasm of cycling myogenic cells and migrates to the nucleus upon induction of the differentiation program. Furthermore, using human RPB3 as bait in a yeast two-hybrid system, we have isolated a novel RPB3 cytoplasmic interacting protein, HCR. HCR, previously identified as α-helix coiled-coil rod homologue, is one of the psoriasis vulgaris (PV) candidate genes. In cycling myogenic C2C7 cells, we show that the RPB3 protein directly interacts with HCR within the cytoplasm. Finally, knocking down HCR expression by RNA interference, we demonstrate that HCR acts as cytoplasmic docking site for RPB3.

Original languageEnglish
Pages (from-to)4253-4260
Number of pages8
JournalJournal of Cell Science
Volume118
Issue number18
DOIs
Publication statusPublished - Sep 15 2005

Keywords

  • HCR
  • Muscle differentiation
  • Psoriasis vulgaris
  • RNAP II
  • RPB3
  • SBP

ASJC Scopus subject areas

  • Cell Biology

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