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

被引：21

作者：

French, Samuel W.

Dawson, David W.

Chen, Hsiao-Wen

Rainey, Robert N.

Sievers, Stuart A.

Balatoni, Cynthia E.

Wong, Larry

Troke, Joshua J.

Nguyen, Mal T. N.

Koehler, Carla M.

Teitell, Michael A. ^{[1
]}

机构：

[1] Univ Calif Los Angeles, David Geffen Sch Med, Dept Pathol & Lab Med, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA

[4] Univ Calif Los Angeles, Jonsson Comprehens Canc Ctr, Los Angeles, CA 90095 USA

来源：

CANCER LETTERS | 2007年 / 248卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

TCL1; PNPase; exoribonuclease; mass spectrometry; leukemia; lymphoma;

D O I：

10.1016/j.canlet.2006.07.006

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 [肿瘤学];

摘要：

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. (c) 2006 Elsevier Ireland Ltd. All rights reserved.

引用

页码：198 / 210

页数：13

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