Cell Biochemistry and Biophysics

, Volume 39, Issue 2, pp 119–131

Distinct domains of human CDC5 direct its nuclear import and association with the spliceosome

Authors

  • Liansen Liu
    • Cardiovascular Research InstituteUniversity of California San Francisco
  • Remo Gräub
    • Cardiovascular Research InstituteUniversity of California San Francisco
  • Myint Hlaing
    • Cardiovascular Research InstituteUniversity of California San Francisco
  • Conrad L. Epting
    • Cardiovascular Research InstituteUniversity of California San Francisco
    • Department of PediatricsUniversity of California San Francisco
  • Christoph W. Turck
    • Howard Hughes Medical InstituteUniversity of California San Francisco
  • Xiao-Qin Xu
    • Department of PediatricsUniversity of California San Francisco
  • Leanne Zhang
    • Cardiovascular Research InstituteUniversity of California San Francisco
    • Cardiovascular Research InstituteUniversity of California San Francisco
    • Cancer CenterUniversity of California San Francisco
    • Department of PediatricsUniversity of California San Francisco
Original Article

DOI: 10.1385/CBB:39:2:119

Cite this article as:
Liu, L., Gräub, R., Hlaing, M. et al. Cell Biochem Biophys (2003) 39: 119. doi:10.1385/CBB:39:2:119

Abstract

Genetic studies have shown that CDC5 proteins are essential for G2 progression and mitotic entry. CDC5 homologs in yeast and mammals are essential for pre-messenger ribonucleic acid (mRNA) processing. Other gene products also have been shown to play roles in both pre-mRNA splicing and cell cycle regulation, prompting the description of several models to explain the mechanism(s) linking these two processes. In this study, we demonstrate that the amino-terminus of human CDC5 directs nuclear import independent of consensus nuclear localization signals or phosphorylation, and that the carboxyl-terminus of human CDC5 preferentially associates with spliceosomal complexes in proximity of RNA transcription during interphase. hCDC5 colocalizes with Sm proteins in a cell cycle- and domain-dependent manner, and several proteins in the human CDC5-associated complex are identified that suggest potential roles for the complex in coupling pre-mRNA splicing to transcriptional activation and protein translation. These results indicate that human CDC5 may function in pre-mRNA processing and cell cycle progression through more than one mechanism.

Index Entries

Cell cyclenuclear specklenuclear importphosphorylationpre-mRNA splicingspliceosome

Copyright information

© Humana Press Inc 2003