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First published online 1 September 2005
doi: 10.1242/jcs.02545

Journal of Cell Science 118, 4253-4260 (2005)
Published by The Company of Biologists 2005
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Research Article

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

Nicoletta Corbi1, Tiziana Bruno2, Roberta De Angelis2, Monica Di Padova2, Valentina Libri1, Maria Grazia Di Certo1,3, Laura Spinardi4, Aristide Floridi3, Maurizio Fanciulli2,5 and Claudio Passananti1,5,*

1 Istituto di Biologia e Patologia Molecolari CNR, Universita' di Roma `La Sapienza', P. le A. Moro, 5, 00185 Roma, Italy
2 Laboratory `B', Regina Elena Cancer Institute, Via delle Messi d'Oro 156, 00158 Rome, Italy
3 Department of Experimental Medicine, Via Vetoio, Coppito 2, University of L'Aquila, 67100 L'Aquila, Italy
4 Department of Biotechnology and Biosciences, University of Milano Bicocca, Piazza della Scienza 2, 20146 Milano, Italy
5 AIRC-Roman Oncogenomic Center-(ROC), Via delle Messi d'Oro 156, 00158 Rome, Italy

* Author for correspondence (e-mail: claudio.passananti{at}ibpm.cnr.it)

Accepted 14 June 2005

Here, we show that the subcellular localization of {alpha}-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 {alpha}-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.

Key words: RPB3, RNAP II, HCR, SBP, Psoriasis vulgaris, Muscle differentiation


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