Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.
Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.
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TRAPPII 复合物组装和 GTPase Ypt31/32 特异性激活的结构基础。
DOI:
10.1126/sciadv.abi5603
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发表时间:
2022-01-28
期刊:
影响因子:
13.6
通讯作者:
Sui SF
中科院分区:
文献类型:
--
作者:
Mi C;Zhang L;Huang G;Shao G;Yang F;You X;Dong MQ;Sun S;Sui SF
Transport protein particle (TRAPP) complexes belong to the multiprotein tethering complex and exist in three forms—core TRAPP/TRAPPI, TRAPPII, and TRAPPIII. TRAPPII activates GTPase Ypt31/Ypt32 as the guanine nucleotide exchange factor in the trans-Golgi network to determine the maturation of Golgi cisternae into post-Golgi carriers in yeast. Here, we present cryo-EM structures of yeast TRAPPII in apo and Ypt32-bound states. All the structures show a dimeric architecture assembled by two triangle-shaped monomers, while the monomer in the apo state exhibits both open and closed conformations, and the monomer in the Ypt32-bound form only captures the closed conformation. Located in the interior of the monomer, Ypt32 binds with both core TRAPP/TRAPPI and Trs120 via its nucleotide-binding domain and binds with Trs31 via its hypervariable domain. Combined with functional analysis, the structures provide insights into the assembly of TRAPPII and the mechanism of the specific activation of Ypt31/Ypt32 by TRAPPII. Structures of TRAPPII in different states reveal the mechanism of the specific activation of Ypt32 by TRAPPII.
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影响因子:
48
作者:
Kucukelbir, Alp;Sigworth, Fred J.;Tagare, Hemant D.
通讯作者:
Tagare, Hemant D.
DOI:
10.1107/s2059798318009324
发表时间:
2018-09-01
期刊:
Acta crystallographica. Section D, Structural biology
影响因子:
--
作者:
Afonine PV;Klaholz BP;Moriarty NW;Poon BK;Sobolev OV;Terwilliger TC;Adams PD;Urzhumtsev A
通讯作者:
Urzhumtsev A
影响因子:
33.6
作者:
Hutagalung AH;Novick PJ
通讯作者:
Novick PJ
影响因子:
14.8
作者:
Kelley LA;Mezulis S;Yates CM;Wass MN;Sternberg MJ
通讯作者:
Sternberg MJ
影响因子:
3.3
作者:
Jones, S;Newman, C;Segev, N
通讯作者:
Segev, N