Membrane association of the Arabidopsis ARF exchange factor GNOM involves interaction of conserved domains

被引:36
作者
Anders, Nadine [1 ]
Nielsen, Michael [2 ]
Keicher, Jutta [1 ]
Stierhof, York-Dieter [1 ]
Furutani, Masahiko [3 ]
Tasaka, Masao [3 ]
Skriver, Karen [2 ]
Juergens, Gerd [1 ]
机构
[1] Univ Tubingen, Ctr Mol Biol Plants, D-72076 Tubingen, Germany
[2] Univ Copenhagen, Inst Mol Biol & Physiol, DK-2100 Copenhagen, Denmark
[3] Nara Inst Sci & Technol, Nara 6300192, Japan
关键词
D O I
10.1105/tpc.107.056515
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The GNOM protein plays a fundamental role in Arabidopsis thaliana development by regulating endosome-to-plasma membrane trafficking required for polar localization of the auxin efflux carrier PIN1. GNOM is a family member of large ARF guanine nucleotide exchange factors (ARF-GEFs), which regulate vesicle formation by activating ARF GTPases on specific membranes in animals, plants, and fungi. However, apart from the catalytic exchange activity of the SEC7 domain, the functional significance of other conserved domains is virtually unknown. Here, we show that a distinct N-terminal domain of GNOM mediates dimerization and in addition interacts heterotypically with two other conserved domains in vivo. In contrast with N-terminal dimerization, the heterotypic interaction is essential for GNOM function, as mutations abolishing this interaction inactivate the GNOM protein and compromise its membrane association. Our results suggest a general model of large ARF-GEF function in which regulated changes in protein conformation control membrane association of the exchange factor and, thus, activation of ARFs.
引用
收藏
页码:142 / 151
页数:10
相关论文
共 46 条
[1]   The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site [J].
Amor, JC ;
Swails, J ;
Zhu, XJ ;
Roy, CR ;
Nagai, H ;
Ingmundson, A ;
Cheng, XD ;
Kahn, RA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (02) :1392-1400
[2]  
AMOR JC, 1994, NATURE, V372, P704, DOI 10.1038/372704a0
[3]   Hijacking components of the cellular secretory pathway for replication of poliovirus RNA [J].
Belov, George A. ;
Altan-Bonnet, Nihal ;
Kovtunovych, Gennadiy ;
Jackson, Catherine L. ;
Lippincott-Schwartz, Jennifer ;
Ehrenfeld, Ellie .
JOURNAL OF VIROLOGY, 2007, 81 (02) :558-567
[4]   A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the β-phosphate to destabilize GDP on ARF1 [J].
Béraud-Dufour, S ;
Robineau, S ;
Chardin, P ;
Paris, S ;
Chabre, M ;
Cherfils, J ;
Antonny, B .
EMBO JOURNAL, 1998, 17 (13) :3651-3659
[5]   The PH superfold: a structural scaffold for multiple functions [J].
Blomberg, N ;
Baraldi, E ;
Nilges, M ;
Saraste, M .
TRENDS IN BIOCHEMICAL SCIENCES, 1999, 24 (11) :441-445
[6]  
Busch M, 1996, MOL GEN GENET, V250, P681, DOI 10.1007/s004380050121
[7]   A novel Golgi membrane protein is a partner of the ARF exchange factors Gealp and Gea2p [J].
Chantalat, S ;
Courbeyrette, R ;
Senic-Matuglia, F ;
Jackson, CL ;
Goud, B ;
Peyroche, A .
MOLECULAR BIOLOGY OF THE CELL, 2003, 14 (06) :2357-2371
[8]   Structure of the Sec7 domain of the Arf exchange factor ARNO [J].
Cherfils, J ;
Ménétrey, J ;
Mathieu, M ;
La Bras, G ;
Robineau, S ;
Béraud-Dufour, S ;
Antonny, B ;
Chardin, P .
NATURE, 1998, 392 (6671) :101-105
[9]   Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers [J].
Cox, R ;
Mason-Gamer, RJ ;
Jackson, CL ;
Segev, N .
MOLECULAR BIOLOGY OF THE CELL, 2004, 15 (04) :1487-1505
[10]   The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin transport, and auxin-dependent plant growth [J].
Geldner, N ;
Anders, N ;
Wolters, H ;
Keicher, J ;
Kornberger, W ;
Muller, P ;
Delbarre, A ;
Ueda, T ;
Nakano, A ;
Jürgens, G .
CELL, 2003, 112 (02) :219-230