On the action of Brefeldin A on Sec7-stimulated membrane-recruitment and GDP/GTP exchange of Arf proteins

被引:29
作者
Cherfils, J
Melançon, P
机构
[1] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France
[2] Univ Alberta, Dept Cell Biol, Edmonton, AB T6G 2H7, Canada
关键词
Arf protein; Brefeldin A; E/K mutation; GDP/GTP exchange; guanine nucleotide-exchange factor (GEF); Sec; 7; domain;
D O I
10.1042/BST0330635
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
Arf (ADP-ribosylation factor) proteins form a special class of small GTP-binding proteins in that their activation by GDP/GTP exchange is coupled to their recruitment to membranes using a built-in structural mechanism. These coupled processes are stimulated by GEFS (guanine nucleotide-exchange factors) that carry a catalytic Sec7 domain, whose basic mechanism has been uncovered by biochemical and structural studies. Crystal structures of intermediates of the GDP/GTP exchange reaction, from which GDP has not dissociated, notably allowed a movie of the exchange reaction to be reconstituted. They showed that Sec7 domains secure Arf-GDP to membranes before they proceed to nucleotide dissociation, and thus are active participants to the coupling of membrane-recruitment to nucleotide exchange. The drug BFA (Brefeldin A) was used to trap the complex that initiates the exchange reaction, providing a structural basis for its inhibition of Arf and its action on the membrane-recruitment of isolated Sec7 domains. Based on the dissection of this basic mechanism, the survey of reported BFA effects in cells on large multidomain ArfGEFs of the BIG1/2 and GBF1 families shows that the levels and compartmental distribution of BFA-induced recruitment of ArfGEFs to membranes cannot be explained from isolated Sec7 domains acting as independent domains. This leads to the hypothesis that Sec7 activity is inhibited in these ArfGEFs by an intramolecular interaction, which would be released by interaction with a compartment-specific receptor.
引用
收藏
页码:635 / 638
页数:4
相关论文
共 26 条
[1]   N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange [J].
Antonny, B ;
BeraudDufour, S ;
Chardin, P ;
Chabre, M .
BIOCHEMISTRY, 1997, 36 (15) :4675-4684
[2]   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
[3]   Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide exchange [J].
Béraud-Dufour, S ;
Paris, S ;
Chabre, M ;
Antonny, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (53) :37629-37636
[4]   A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains [J].
Chardin, P ;
Paris, S ;
Antonny, B ;
Robineau, S ;
BeraudDufour, S ;
Jackson, CL ;
Chabre, M .
NATURE, 1996, 384 (6608) :481-484
[5]   The role of ARF and Rab GTPases in membrane transport [J].
Chavrier, P ;
Goud, B .
CURRENT OPINION IN CELL BIOLOGY, 1999, 11 (04) :466-475
[6]   GBF1:: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5 [J].
Claude, A ;
Zhao, BP ;
Kuziemsky, CE ;
Dahan, S ;
Berger, SJ ;
Yan, JP ;
Armold, AD ;
Sullivan, EM ;
Melançon, P .
JOURNAL OF CELL BIOLOGY, 1999, 146 (01) :71-84
[7]   BREFELDIN-A INHIBITS GOLGI MEMBRANE-CATALYZED EXCHANGE OF GUANINE-NUCLEOTIDE ONTO ARF PROTEIN [J].
DONALDSON, JG ;
FINAZZI, D ;
KLAUSNER, RD .
NATURE, 1992, 360 (6402) :350-352
[8]   BINDING OF ARF AND BETA-COP TO GOLGI MEMBRANES - POSSIBLE REGULATION BY A TRIMERIC G-PROTEIN [J].
DONALDSON, JG ;
KAHN, RA ;
LIPPINCOTTSCHWARTZ, J ;
KLAUSNER, RD .
SCIENCE, 1991, 254 (5035) :1197-1199
[9]   Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis [J].
Goldberg, J .
CELL, 1999, 96 (06) :893-902
[10]   Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching [J].
Goldberg, J .
CELL, 1998, 95 (02) :237-248