Evidence map›Paper›PMID 38478018›Full record

ArticleThe Journal of cell biology2024

SNARE chaperone Sly1 directly mediates close-range vesicle tethering.

Mengtong Duan, Rachael L Plemel, Tomoka Takenaka, Ariel Lin, Beatriz Marie Delgado, Una Nattermann, Daniel P Nickerson, Joji Mima, Elizabeth A Miller, Alexey J Merz

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

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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

10 authors at 5 institutions in 3 countries.

Mengtong Duan *Department of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0002-1601-8876
Rachael L Plemel *Department of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0009-0001-8583-4164
Tomoka TakenakaTokyo Institute of Technology , Tokyo, Japan.ORCID 0000-0003-3164-4450
Ariel LinDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0009-0000-0443-3987
Beatriz Marie DelgadoDepartment of Biology, California State University, San Bernardino, CA, USA.ORCID 0009-0000-5012-3795
Una NattermannDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0001-7837-7113
Daniel P NickersonDepartment of Biology, California State University, San Bernardino, CA, USA.ORCID 0000-0001-6698-4223
Joji MimaInstitute for Protein Research, Osaka University , Osaka, Japan.ORCID 0000-0002-0454-8669
Elizabeth A MillerMRC Laboratory of Molecular Biology , Cambridge, England.ORCID 0000-0002-1033-8369
Alexey J MerzDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0003-2177-6492
University of Washington · USCalifornia State University, San Bernardino · USMRC Laboratory of Molecular Biology · GBProtein Research Foundation · JPTokyo Institute of Technology · JP

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
CSU San Bernardino Minority Access to Research CareersT34GM083883 · NIGMS · CALIFORNIA STATE UNIV SAN BERNARDINO · PI MCDOUGALL, SANDERS · 2009 to 2019
$3.0M
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
Medical Research Council MC_UP_1201/10NIGMS NIH HHS R01 GM077349NIGMS NIH HHS R01 GM130644NIGMS NIH HHS T32 GM007270NIGMS NIH HHS T34 GM083883NIH HHS R01 GM077349
6 · The paper itself

Abstract

The essential Golgi protein Sly1 is a member of the Sec1/mammalian Unc-18 (SM) family of SNARE chaperones. Sly1 was originally identified through remarkable gain-of-function alleles that bypass requirements for diverse vesicle tethering factors. Employing genetic analyses and chemically defined reconstitutions of ER-Golgi fusion, we discovered that a loop conserved among Sly1 family members is not only autoinhibitory but also acts as a positive effector. An amphipathic lipid packing sensor (ALPS)-like helix within the loop directly binds high-curvature membranes. Membrane binding is required for relief of Sly1 autoinhibition and also allows Sly1 to directly tether incoming vesicles to the Qa-SNARE on the target organelle. The SLY1-20 mutation bypasses requirements for diverse tethering factors but loses this ability if the tethering activity is impaired. We propose that long-range tethers, including Golgins and multisubunit tethering complexes, hand off vesicles to Sly1, which then tethers at close range to initiate trans-SNARE complex assembly and fusion in the early secretory pathway.

Indexed as

Cytoplasmic VesiclesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAnimalsGolgi ApparatusMammalsMolecular ChaperonesMunc18 ProteinsSNARE ProteinsVesicular Transport ProteinsMolecular ChaperonesMunc18 ProteinsSaccharomyces cerevisiae ProteinsSLY1 protein, S cerevisiaeSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID38478018
PMCPMC10943277
OpenAlexW4392740417

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.