p29, a novel GCIP-interacting protein, localizes in the nucleus

Biochem Biophys Res Commun. 2000 Dec 20;279(2):732-7. doi: 10.1006/bbrc.2000.3992.

Abstract

GCIP, a newly identified cyclin D-interacting protein, was found to reduce the phosphorylation of retinoblastoma protein and inhibit E2F1-mediated transcriptional activity. To explore more GCIP interacting proteins, the yeast two-hybrid screening using GCIP as a bait protein was performed. One novel gene, p29, was demonstrated to associate with GCIP in the yeast two-hybrid method and in vitro GST pull-down assay. Multiple tissue Northern blot analysis showed that p29 was abundantly expressed in the heart, skeletal muscle, and kidney relative to other tissues. The transient expression of HA-tagged p29 in HeLa cells localized in the nucleus. Taken together, we have isolated a novel protein, p29, which may be involved in the functional regulation of GCIP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Cyclin D
  • Cyclins / metabolism
  • Glutathione Transferase / genetics
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism*
  • Open Reading Frames
  • Protein Biosynthesis
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*

Substances

  • CCNDBP1 protein, human
  • Cyclin D
  • Cyclins
  • GCIP-interacting protein p29, human
  • Nuclear Proteins
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Transcription Factors
  • Glutathione Transferase