HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Collart, C. Articles by Verschueren, K. Search for Related Content PubMed PubMed Citation Articles by Collart, C. Articles by Verschueren, K.

¹ Department of Developmental Biology (VIB-07), Flanders Interuniversity Institute for Biotechnology (VIB), and Laboratory of Molecular Biology (Celgen), University of Leuven, B-3000 Leuven, Belgium
² Department of Cell Biology, Biozentrum, University of Basel, CH-4056, Switzerland

Ligand-bound receptors of the Transforming Growth Factor-ß (TGF-ß) family promote the formation of complexes between Smad proteins that subsequently accumulate in the nucleus and interact there with other transcriptional regulators, leading to modulation of target gene expression. We identified a novel nuclear protein, Smicl, which binds to Smad proteins. Smicl and Smads cooperate and enhance TGF-ß mediated activation of a Smad-responsive reporter gene. A domain with five CCCH-type zinc fingers in Smicl is structurally and functionally, at least in vitro, similar to a domain in CPSF-30, the 30 kDa subunit of Cleavage and Polyadenylation Specificity Factor (CPSF). Like CPSF-30, Smicl can associate with some other CPSF subunits characterized previously. Its effect on the induction of a reporter gene for TGF-ß requires the cleavage/polyadenylation signal downstream of the coding sequence of that gene. Thus, Smicl is a novel protein that displays CPSF-30-like activities, interacts in the nucleus with activated Smads, and potentiates in TGF-ß stimulated cells Smad-dependent transcriptional responses, possibly in conjunction with the activity of CPSF complexes.

Present addresses: ^aDipartimento di Biotechnologie e Bioscienze, Università di Milano-Bicocca, Piazza della Scienza 2, Milano, Italy;

^bJanssen Research Foundation, Turnhoutsesteenweg 30, B-2340 Beerse, Belgium.

^* Correspondence: E-mail: kristin{at}med.kuleuven.ac.be

This article has been cited by other articles:

				C. Collart, J. M. Ramis, T. A. Down, and J. C. Smith Smicl is required for phosphorylation of RNA polymerase II and affects 3'-end processing of RNA at the midblastula transition in Xenopus Development, October 15, 2009; 136(20): 3451 - 3461. [Abstract] [Full Text] [PDF]

				J. A. Hurt, R. A. Obar, B. Zhai, N. G. Farny, S. P. Gygi, and P. A. Silver A conserved CCCH-type zinc finger protein regulates mRNA nuclear adenylation and export J. Cell Biol., April 20, 2009; 185(2): 265 - 277. [Abstract] [Full Text] [PDF]

				H. Peeters, M. L. Voz, K. Verschueren, B. De Cat, H. Pendeville, B. Thienpont, A. Schellens, J. W. Belmont, G. David, W. J.M. Van De Ven, et al. Sesn1 is a novel gene for left-right asymmetry and mediating nodal signaling Hum. Mol. Genet., November 15, 2006; 15(22): 3369 - 3377. [Abstract] [Full Text] [PDF]

				C. Collart, K. Verschueren, A. Rana, J. C. Smith, and D. Huylebroeck The novel Smad-interacting protein Smicl regulates Chordin expression in the Xenopus embryo Development, October 15, 2005; 132(20): 4575 - 4586. [Abstract] [Full Text] [PDF]