• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo.

The PITSLRE protein kinases are members of the p34cdc2 superfamily, with >20 different isoforms expressed from two linked genes in humans. PITSLRE homologues have been identified in mouse, chicken, Drosophila, Xenopus, and possibly Plasmodium falciparum, suggesting that their function may be well conserved. A possible role for a caspase processed PITSLRE isoform has been suggested by studies of Fas- and TNF-induced cell death. However, the function of these kinases in proliferating cells is still unknown. Here we demonstrate that the 110 kDa PITSLRE isoforms (p110) are localized to both the nucleoplasm and nuclear speckles, and that these isoforms specifically interact in vitro and in vivo with the RNA-binding protein RNPS1. RNPS1 is also localized to nuclear speckles, and its over expression disrupts normal nuclear speckle organization by causing the aggregation of many nuclear speckles into approximately 6 'mega' speckles. This type of nuclear speckle aggregation closely resembles what occurs when cells are treated with several transcriptional inhibitors. These data indicate that the PITSLRE p110 isoforms interact with RNPS1 in vivo, and that these proteins may in turn influence some aspect of transcriptional and/or splicing regulation.

Pubmed ID: 9580558

Authors

  • Loyer P
  • Trembley JH
  • Lahti JM
  • Kidd VJ

Journal

Journal of cell science

Publication Data

June 28, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: 5 T32 CA09346
  • Agency: NCI NIH HHS, Id: CA21765
  • Agency: NIGMS NIH HHS, Id: GM44088

Mesh Terms

  • Animals
  • CDC2 Protein Kinase
  • Cyclin-Dependent Kinases
  • DNA-Binding Proteins
  • HeLa Cells
  • Humans
  • Mice
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • Signal Transduction
  • Transcription, Genetic