Nuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP)

被引：18

作者：

El Bounkari, Omar ^{[1
]}

Guria, Anuja ^{[1
]}

Klebba-Faerber, Sabine ^{[1
]}

Claussen, Maike ^{[2
]}

Pieler, Tomas ^{[2
]}

Griffiths, John R. ^{[3
]}

Whetton, Anthony D. ^{[3
]}

Koch, Alexandra ^{[1
]}

Tamura, Teruko ^{[1
]}

机构：

[1] OE4310 Med Hsch Hannover, Inst Biochem, D-30623 Hannover, Germany

[2] Univ Gottingen, Zentrum Biochem & Mol Zellbiol, Abt Entwicklungsbiochemie, D-37077 Gottingen, Germany

[3] Univ Manchester, Christie Hosp, Fac Med & Human Sci, Sch Canc & Imaging Sci, Manchester M20 9BX, Lancs, England

来源：

FEBS LETTERS | 2009年 / 583卷 / 01期

关键词：

FMIP/THOC5/fSAP79; THOC7/fSAP24; mRNA processing complex; Nucleocytoplasmic shuttling protein; TRANSCRIPTIONAL ELONGATION; GENOME INSTABILITY; COMPLEX; EXPORT; RECEPTOR; CELLS; TREX; DIFFERENTIATION; RECOMBINATION; REQUIREMENTS;

D O I：

10.1016/j.febslet.2008.11.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

THOC7 and Fms-interacting protein (FMIP) are members of the THO complex that associate with the mRNA export apparatus. FMIP is a nucleocytoplasmic shuttling protein with a nuclear localization signal (NLS), whereas THOC7 does not contain a typical NLS motif. We show here that THOC7 (50-137, amino acid numbers) binds to the N-terminal portion (1-199) of FMIP directly. FMIP is detected mainly in the nucleus. In the absence of exogenous FMIP, THOC7 resides mainly in the cytoplasm, while in the presence of FMIP, THOC7 is transported into the nucleus with FMIP. Furthermore, THOC7 lacking the FMIP binding site does not co-localize with FMIP, indicating that THOC7/FMIP interaction is required for nuclear localization of THOC7.

引用

页码：13 / 18

页数：6

共 20 条

[1]

A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae [J].

Chávez, S ;

Beilharz, T ;

Rondón, AG ;

Erdjument-Bromage, H ;

Tempst, P ;

Svejstrup, JQ ;

Lithgow, T ;

Aguilera, A .

EMBO JOURNAL, 2000, 19 (21) :5824-5834

[2]

The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability [J].

Chávez, S ;

Aguilera, A .

GENES & DEVELOPMENT, 1997, 11 (24) :3459-3470

[3]

Human mRNA export machinery recruited to the 5′ end of mRNA [J].

Cheng, Hong ;

Dufu, Kobina ;

Lee, Chung-Sheng ;

Hsu, Jeanne L. ;

Dias, Anusha ;

Reed, Robin .

CELL, 2006, 127 (07) :1389-1400

[4]

The death domain protein p84N5, but not the short isoform p84N5s, is cell cycle-regulated and shuttles between the nucleus and the cytoplasme [J].

Gasparri, F ;

Sola, F ;

Locatelli, G ;

Muzio, M .

FEBS LETTERS, 2004, 574 (1-3) :13-19

[5]

Novel insulin-elicited phosphoproteins in adipocytes [J].

Gridley, S ;

Lane, WS ;

Garner, CW ;

Lienhard, GE .

CELLULAR SIGNALLING, 2005, 17 (01) :59-66

[6]

The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability [J].

Jimeno, S ;

Rondón, AG ;

Luna, R ;

Aguilera, A .

EMBO JOURNAL, 2002, 21 (13) :3526-3535

[7]

Inhibition of Abl tyrosine kinase enhances nerve growth factor-mediated signaling in Bcr-Abl transformed cells via the alteration of signaling complex and the receptor turnover [J].

Koch, A. ;

Scherr, M. ;

Breyer, B. ;

Mancini, A. ;

Kardinal, C. ;

Battmer, K. ;

Eder, M. ;

Tamura, T. .

ONCOGENE, 2008, 27 (34) :4678-4689

[8]

Cancer cells and normal cells differ in their requirements for Thoc1 [J].

Li, Yanping ;

Lin, Athena W. ;

Zhang, Xiaojing ;

Wang, Yanqing ;

Wang, Xiaoling ;

Goodrich, David W. .

CANCER RESEARCH, 2007, 67 (14) :6657-6664

[9]

FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBPalpha [J].

Mancini, A. ;

El Bounkari, O. ;

Norrenbrock, A-F ;

Scherr, M. ;

Schaefer, D. ;

Eder, M. ;

Banham, A. H. ;

Pulford, K. ;

Lyne, L. ;

Whetton, A. D. ;

Tamura, T. .

ONCOGENE, 2007, 26 (07) :1020-1027

[10]

The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation [J].

Mancini, A ;

Koch, A ;

Whetton, AD ;

Tamura, T .

ONCOGENE, 2004, 23 (39) :6581-6589

← 1 2 →