2. Academic Validation
  3. The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

  • Cancer Lett. 2007 Apr 18;248(2):198-210. doi: 10.1016/j.canlet.2006.07.006.
Samuel W French 1,  David W Dawson,  Hsiao-Wen Chen,  Robert N Rainey,  Stuart A Sievers,  Cynthia E Balatoni,  Larry Wong,  Joshua J Troke,  Mai T N Nguyen,  Carla M Koehler,  Michael A Teitell
Affiliations

Affiliation

  • 1 Department of Pathology and Laboratory Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095-1732, USA.
PMID: 16934922 DOI: 10.1016/j.canlet.2006.07.006
Abstract

TCL1 is an Akt kinase coactivator that, when dysregulated, initiates mature lymphocyte malignancies in humans and transgenic mice. While TCL1 augments Akt pathway signaling, additional TCL1 interacting proteins that may contribute to cellular homeostasis or transformation are lacking. Here, an exoribonuclease, PNPase, was identified in a complex with TCL1. The Akt interaction domain on TCL1 bound either RNase PH repeat domain of PNPase without influencing its RNA degrading activity, which was compatible with predicted docking models for a TCL1-PNPase complex. Our data provide a novel protein interaction for mammalian PNPase that may impact TCL1 mediated transformation.

Figures