The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation.
The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation.
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DOI:
10.1038/nsmb.2414
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发表时间:
2012-12
影响因子:
16.8
通讯作者:
Owen, David J.
中科院分区:
文献类型:
--
作者:
Schaefer, Ingmar B.;Hesketh, Geoffrey G.;Bright, Nicholas A.;Gray, Sally R.;Pryor, Paul R.;Evans, Philip R.;Luzio, J. Paul;Owen, David J.
SNAREs provide energy and specificity to membrane fusion events. Fusogenic trans-SNARE complexes are assembled from Q-SNAREs embedded in one membrane and an R–SNARE embedded in the other. Regulation of membrane fusion events is crucial for intracellular trafficking. We identify the endosomal protein Varp as an R-SNARE-binding regulator of SNARE complex formation. Varp co-localises with and binds to VAMP7, an R-SNARE involved in both endocytic and secretory pathways. We present the structure of the second ankyrin repeat domain of mammalian Varp in complex with the cytosolic portion of VAMP7. The VAMP7 SNARE motif is trapped between Varp and the VAMP7 longin domain and hence Varp kinetically inhibits VAMP7’s ability to form SNARE complexes. This inhibition will be increased when Varp can also bind to other proteins present on the same membrane as the VAMP7 such as Rab32:GTP.
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DOI:
10.1107/s0907444905036693
发表时间:
2006-01-01
影响因子:
2.2
作者:
Evans, P
通讯作者:
Evans, P
影响因子:
2.3
作者:
Liou, W;Geuze, HJ;Slot, JW
通讯作者:
Slot, JW
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
16
作者:
Höning, S;Ricotta, D;Owen, DJ
通讯作者:
Owen, DJ
DOI:
10.1107/s0907444909042073
发表时间:
2010-01
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Chen VB;Arendall WB 3rd;Headd JJ;Keedy DA;Immormino RM;Kapral GJ;Murray LW;Richardson JS;Richardson DC
通讯作者:
Richardson DC