Evidence map›Paper›PMID 38478017›Full record

ArticleThe Journal of cell biology2024

SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.

Mengtong Duan, Guanbin Gao, Ariel Lin, Emma J Mackey, David K Banfield, Alexey J Merz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 46% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Two-Step Engineering of Food-GradeJournal of fungi (Basel, Switzerland) · 2026
    Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Mengtong DuanDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0002-1601-8876
Guanbin GaoThe Division of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong Kong.ORCID 0000-0002-3766-6231
Ariel LinDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0009-0000-0443-3987
Emma J MackeyDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0003-3408-5332
David K BanfieldThe Division of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong Kong.ORCID 0000-0002-5492-5741
Alexey J MerzDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0003-2177-6492
University of Washington · USHong Kong University of Science and Technology · HK

Funding

Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
MECHANISMS OF AP-3 FUNCTION IN VESICLE FORMATION AND GOLGI MATURATIONR01GM130644 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL, ODORIZZI, CHARLES G · 2019 to 2022
$1.9M
NIGMS NIH HHS R01 GM077349NIGMS NIH HHS R01 GM130644NIH HHS R01 GM077349
6 · The paper itself

Abstract

SM proteins including Sly1 are essential cofactors of SNARE-mediated membrane fusion. Using SNARE and Sly1 mutants and chemically defined in vitro assays, we separate and assess proposed mechanisms through which Sly1 augments fusion: (i) opening the closed conformation of the Qa-SNARE Sed5; (ii) close-range tethering of vesicles to target organelles, mediated by the Sly1-specific regulatory loop; and (iii) nucleation of productive trans-SNARE complexes. We show that all three mechanisms are important and operate in parallel, and that close-range tethering promotes trans-complex assembly when cis-SNARE assembly is a competing process. Further, we demonstrate that the autoinhibitory N-terminal Habc domain of Sed5 has at least two positive activities: it is needed for correct Sed5 localization, and it directly promotes Sly1-dependent fusion. "Split Sed5," with Habc presented solely as a soluble fragment, can function both in vitro and in vivo. Habc appears to facilitate events leading to lipid mixing rather than promoting opening or stability of the fusion pore.

Indexed as

Membrane FusionMunc18 ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsProtein BindingQa-SNARE ProteinsSaccharomyces cerevisiaeVesicular Transport ProteinsMunc18 ProteinsQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSed5 protein, S cerevisiaeSLY1 protein, S cerevisiaeSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID38478017
PMCPMC10943372
OpenAlexW4392762480

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.