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Collins KM, et al.  (2005) Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J 24(10):1775-86

Abstract: SNARE functions during membrane docking and fusion are regulated by Sec1/Munc18 (SM) chaperones and Rab/Ypt GTPase effectors. These functions for yeast vacuole fusion are combined in the six-subunit HOPS complex. HOPS facilitates Ypt7p nucleotide exchange, is a Ypt7p effector, and contains an SM protein. We have dissected the associations and requirements for HOPS, Ypt7p, and Sec17/18p during SNARE complex assembly. Vacuole SNARE complexes bind either Sec17p or the HOPS complex, but not both. Sec17p and its co-chaperone Sec18p disassemble SNARE complexes. Ypt7p regulates the reassembly of unpaired SNAREs with each other and with HOPS, forming HOPS.SNARE complexes prior to fusion. After HOPS.SNARE assembly, lipid rearrangements are still required for vacuole content mixing. Thus, Sec17p and HOPS have mutually exclusive interactions with vacuole SNAREs to mediate disruption of SNARE complexes or their assembly for docking and fusion. Sec17p may displace HOPS from SNAREs to permit subsequent rounds of fusion.

Status: Published Type: Journal Article PubMed ID: 15889152

Topics addressed in this paper

Number of different genes curated to this paper: 15

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Topics Genes linked to topics (#1 - 10 )
NYV1 PEP3 PEP5 SEC17 SEC18 VAM3 VAM6 VAM7 VPS16 VPS3
Cellular Location blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball
Function/Process blue ball blue ball blue ball blue ball blue ball blue ball
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Topics Genes linked to topics (#11 - 15 )
VPS33 VPS41 VTI1 YKT6 YPT7
Cellular Location blue ball blue ball blue ball blue ball blue ball
Function/Process blue ball blue ball blue ball
Primary Literature blue ball blue ball blue ball blue ball blue ball
Protein-protein Interactions blue ball blue ball blue ball blue ball blue ball
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