Evidence map›Paper›PMID 19713939›Full record

ArticleThe EMBO journal2009

Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.

Amanda Reider, Sarah L Barker, Sanjay K Mishra, Young Jun Im, Lymarie Maldonado-Báez, James H Hurley, Linton M Traub, Beverly Wendland

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

97 citing papers in PubMed, 164 citations in OpenAlex.

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  13. Linton Mark Traub (1962-2020).The Journal of cell biology · 2021
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37 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

Amanda ReiderDepartment of Biology, The Johns Hopkins University, Baltimore, MD 21218-2685, USA.
Sarah L Barker
Sanjay K Mishra
Young Jun Im
Lymarie Maldonado-Báez
James H Hurley
Linton M Traub
Beverly Wendland
Johns Hopkins University · USNational Institutes of Health · USUniversity of Pittsburgh · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
MOLECULAR ANALYSIS OF ENDOCYTOSIS PROTEINS IN YEASTR01GM060979 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WENDLAND, BEVERLY R · 2000 to 2013
$4.3M
CLATHRIN COATED VESICLES AND LYSOSOME FUNCTIONR01DK053249 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TRAUB, LINTON M. · 1998 to 2011
$3.0M
Molecular Recognition by Clathrin AdaptorsZIADK036130 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HURLEY, JAMES · 2009 to 2013
$1.3M
Intramural NIH HHSNIDDK NIH HHS R01 DK053249NIDDK NIH HHS R01 DK53249NIGMS NIH HHS GM07231NIGMS NIH HHS R01 GM060979NIGMS NIH HHS R01 GM60979NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding mu homology domains (muHDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The muHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.

Indexed as

EndocytosisHeLa CellsHumansMembrane ProteinsProtein BindingProteinsProtein Structure, SecondarySaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesEde1 protein, S cerevisiaeFCHO1 protein, humanMembrane ProteinsProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19713939
PMCPMC2771086
OpenAlexW2077084337

What OpenQuestion holds

Textmetadata
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.