How Tlg2p/syntaxin 16 'snares' Vps45

被引:148
作者
Dulubova, I
Yamaguchi, T
Gao, Y
Min, SW
Huryeva, I
Südhof, TC
Rizo, J
机构
[1] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA
[2] Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75390 USA
[3] Univ Texas, SW Med Ctr, Ctr Basic Neurosci, Dept Mol Genet, Dallas, TX 75390 USA
[4] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA
关键词
SM proteins; SNAREs; syntaxins; Tlg2p; Vps45p;
D O I
10.1093/emboj/cdf381
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
Soluble N-ethylmaleimide sensitive factor-attachment protein receptors (SNAREs) and Sec1p/Munc18-homologs (SM proteins) play key roles in intracellular membrane fusion. The SNAREs form tight four-helix bundles (core complexes) that bring the membranes together, but it is unclear how this activity is coupled to SM protein function. Studies of the yeast trans-Golgi network (TGN)/endosomal SNARE complex, which includes the syntaxin-like SNARE Tlg2p, have suggested that its assembly requires activation by binding of the SM protein Vps45p to the cytoplasmic region of Tlg2p folded into a closed conformation. Nuclear magnetic resonance and biochemical experiments now show that Tlg2p and Pep12p, a late- endosomal syntaxin that interacts functionally but not directly with Vps45p, have a domain structure characteristic of syntaxins but do not adopt a closed conformation. Tlg2p binds tightly to Vps45p via a short N-terminal peptide motif that is absent in Pep12p. The Tlg2p/Vps45p binding mode is shared by the mammalian syntaxin 16, confirming that it is a Tlg2p homolog, and resembles the mode of interaction between the SM protein Sly1p and the syntaxins Ufe1p and Sed5p. Thus, this mechanism represents the most widespread mode of coupling between syntaxins and SM proteins.
引用
收藏
页码:3620 / 3631
页数:12
相关论文
共 56 条
[1]   Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p [J].
Abeliovich, H ;
Darsow, T ;
Emr, SD .
EMBO JOURNAL, 1999, 18 (21) :6005-6016
[2]   Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures [J].
Abeliovich, H ;
Grote, E ;
Novick, P ;
Ferro-Novick, S .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (19) :11719-11727
[3]   AtVPS45 complex formation at the trans-Golgi network [J].
Bassham, DC ;
Sanderfoot, AA ;
Kovaleva, V ;
Zheng, HY ;
Raikhel, NV .
MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (07) :2251-2265
[4]   THE MOLECULAR MACHINERY FOR SECRETION IS CONSERVED FROM YEAST TO NEURONS [J].
BENNETT, MK ;
SCHELLER, RH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (07) :2559-2563
[5]   The Tlg SNARE complex is required for TGN homotypic fusion [J].
Brickner, JH ;
Blanchette, JM ;
Sipos, G ;
Fuller, RS .
JOURNAL OF CELL BIOLOGY, 2001, 155 (06) :969-978
[6]   Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation [J].
Bryant, NJ ;
James, DE .
EMBO JOURNAL, 2001, 20 (13) :3380-3388
[7]   A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast [J].
Burd, CG ;
Peterson, M ;
Cowles, CR ;
Emr, SD .
MOLECULAR BIOLOGY OF THE CELL, 1997, 8 (06) :1089-1104
[8]   A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60 [J].
Cao, XW ;
Südhof, TC .
SCIENCE, 2001, 293 (5527) :115-120
[9]   Sec1p binds to SNARE complexes and concentrates at sites of secretion [J].
Carr, CM ;
Grote, E ;
Munson, M ;
Hughson, FM ;
Novick, PJ .
JOURNAL OF CELL BIOLOGY, 1999, 146 (02) :333-344
[10]   A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae [J].
Coe, JGS ;
Lim, ACB ;
Xu, J ;
Hong, WJ .
MOLECULAR BIOLOGY OF THE CELL, 1999, 10 (07) :2407-2423