PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain

M. Waragai, E. Junn, M. Kajikawa, S. Takeuchi, I. Kanazawa, M. Shibata, M. M. Mouradian, H. Okazawa

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

PQBP-1 was identified as a binding protein to the polyglutamine tract present in various transcription-related factors and causative genes for neurodegenerative disorders. This novel gene contains at least two functional domains, WW domain and carboxyl-terminal domain (CTD), strictly conserved beyond species. Although human PQBP-1 additionally contains the polar amino acid-rich domain by which it binds to the polyglutamine tract, genuine physiological function(s) have not been clarified. In this study, we showed that U5-15kD, human homologue of fission yeast dim1p, is a partner molecule of PQBP-1 binding to CTD. This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)592-595
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume273
Issue number2
DOIs
StatePublished - Jul 5 2000

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biophysics
  • Biochemistry
  • Cell Biology

Fingerprint

Dive into the research topics of 'PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain'. Together they form a unique fingerprint.

Cite this