The Habc Domain of the SNARE Vam3 Interacts with the HOPS Tethering Complex to Facilitate Vacuole Fusion

Lürick, Anna; Kuhlee, Anne; Bröcker, Cornelia; Kümmel, Daniel; Raunser, Stefan; Ungermann, Christian

doi:10.1074/jbc.m114.631465

Cited by 38 publications

(45 citation statements)

References 34 publications

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“…, 2012; Lürick et al. , 2015), tethers such as HOPS use Rab binding to bridge membranes and confer SNARE assembly by recognizing both individual SNAREs and SNARE complexes (Jun et al.…”

Section: Discussionmentioning

confidence: 99%

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Multivalent Rab interactions determine tether-mediated membrane fusion

Lürick

Gao

Kuhlee

et al. 2017

MBoC

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“…, 2012; Lürick et al. , 2015), tethers such as HOPS use Rab binding to bridge membranes and confer SNARE assembly by recognizing both individual SNAREs and SNARE complexes (Jun et al.…”

Section: Discussionmentioning

confidence: 99%

“…Plasmids used for generation of recombinant Ypt7 and SNAREs have been described (Cabrera et al. , 2014; Lürick et al. , 2015).…”

Section: Methodsmentioning

confidence: 99%

Multivalent Rab interactions determine tether-mediated membrane fusion

Lürick

Gao

Kuhlee

et al. 2017

MBoC

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“…These and other data indicate that the essential role of the N-peptide is to recruit the SM protein to the site of SNARE complex assembly. Other Qa-SNAREs, including those that lack an N-peptide, probably recruit SM proteins using alternative or additional strategies 66,93 .…”

Section: Sec1-munc18 Proteins and Snare Assemblymentioning

confidence: 99%

“…2b). The other subunits of the HOPS complex bind to the N-terminal regions of two out of the four SNAREs that are required for vacuolar fusion (Vam3 and Vam7) 64,66,67 . Other MTCs, which are not as tightly associated with an SM protein, could nonetheless create an ‘assembly zone’ in which the SNARE motifs are presented to the cognate SM protein.…”

Section: Sec1-munc18 Proteins and Snare Assemblymentioning

confidence: 99%

Chaperoning SNARE assembly and disassembly

Baker

Hughson

2016

Nat Rev Mol Cell Biol

224

238

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Intracellular membrane fusion is mediated in most cases by membrane-bridging complexes of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). Yet in vitro, the assembly of such complexes is inefficient, and their uncatalyzed disassembly is undetectably slow. Here, we focus on the cellular machinery that orchestrates SNARE complex assembly and disassembly, thereby regulating processes ranging from vesicle trafficking to organelle fusion to neurotransmitter release. Rapid progress is being made on many fronts, including the development of more realistic cell-free reconstitutions, the application of single-molecule biophysics, and the elucidation of x-ray and high-resolution electron microscopy structures of the SNARE assembly and disassembly machineries ‘in action’.

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“…Additionally, mammalian dynamins are implicated in membrane fusion (Reid et al, 2012). Likewise, Vps1 was found to play an important role in homotypic vacuolar fusion (Peters et al, 2004) by inducing the interaction between Vam3 SNARE and the HOPS tethering complex at the vacuole (Kulkarni et al, 2014;Lurick et al, 2015). Furthermore, a recent study showing that loss of Vps1 leads to a robust increase of late Golgi in number indicates that Vps1 may function for homotypic fusion between late Golgi membranes (Goud Gadila et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Yeast dynamin and Ypt6 function in parallel for the endosome‐to‐Golgi retrieval of Snc1

Makaraci

Cruz²,

McDermott

et al. 2019

Cell Biology International

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Protein recycling is an important cellular process required for cell homeostasis. Results from prior studies have shown that Vps1, a dynamin homologue in yeast, is implicated in protein recycling from the endosome to the trans-Golgi Network (TGN). However, the function of Vps1 in relation to Ypt6, a master GTPase in the recycling pathway, remains unknown. The present study reveals that Vps1 physically interacts with Ypt6 if at least one of them is full-length. We found that overexpression of full-length Vps1, but not GTP hydrolysis-defective Vps1 mutants, is sufficient to rescue abnormal phenotypes of Snc1 distribution provoked by loss of Ypt6, and vice versa. This suggests that Vps1 and Ypt6 function in parallel pathways instead of in a sequential pathway, and that GTP binding/hydrolysis of Vps1 is required for proper traffic of Snc1 toward the TGN. Additionally, we identified two novel Vps1 binding partners, Vti1 and Snc2, which function for the endosome-derived vesicle fusion at the TGN. Taken together, the present study demonstrates that Vps1 plays a role in later stages of the endosome-to-TGN traffic.

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The Habc Domain of the SNARE Vam3 Interacts with the HOPS Tethering Complex to Facilitate Vacuole Fusion

Cited by 38 publications

References 34 publications

Multivalent Rab interactions determine tether-mediated membrane fusion

Multivalent Rab interactions determine tether-mediated membrane fusion

Chaperoning SNARE assembly and disassembly

Yeast dynamin and Ypt6 function in parallel for the endosome‐to‐Golgi retrieval of Snc1

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