Evidence map›Paper›PMID 10944111›Full record

ArticleThe EMBO journal2000

An intact SH3 domain is required for myosin I-induced actin polymerization.

M I Geli, R Lombardi, B Schmelzl, H Riezman

Abstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

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  17. Ultrastructural dynamics of proteins involved in endocytic budding.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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

4 authors.

M I GeliBiochemie Zentrum, University of Heidelberg, D-69120 Heidelberg, Germany. maribel.geli@urz.uni-heidelberg.de
R Lombardi
B Schmelzl
H Riezman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast type I myosins (MYO3 and MYO5) are involved in endocytosis and in the polarization of the actin cytoskeleton. The tail of these proteins contains a Tail Homology 2 (TH2) domain that constitutes a putative actin-binding site. Because of the important mechanistic implications of a second ATP-independent actin-binding site, we analyzed its functional relevance in vivo. Even though the myosin tail interacts with actin, and this interaction seems functionally important, deletion of a major portion of the TH2 domain did not abolish interaction. In contrast, we found that the SH3 domain of Myo5p significantly contributes to this interaction, implicating other proteins. We found that Vrp1p, the yeast homolog of WIP [Wiskott-Aldrich syndrome protein (WASP)-interacting protein], seems necessary to sustain the Myo5p tail-F-actin interaction. Consistent with recent results implicating the yeast type I myosins in regulating actin polymerization in vivo, we demonstrate that the C-terminal domain of Myo5p is able to induce cytosol-dependent actin polymerization in vitro, and that this activity requires both an intact Myo5p SH3 domain and Vrp1p.

Indexed as

Myosin Type ISaccharomyces cerevisiae Proteinssrc Homology DomainsActinsAdenosine TriphosphateAllelesBinding SitesCytosolElectrophoresis, Polyacrylamide GelFungal ProteinsGenotypeGlutathione TransferaseImmunoblottingMating FactorMicrofilament ProteinsMyosinsActinsAdenosine TriphosphateFungal ProteinsGlutathione TransferaseMating FactorMicrofilament ProteinsMYO5 protein, S cerevisiaeMyosinsMyosin Type IPeptidesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVRP1 protein, S cerevisiae

Identifiers

PMID10944111
PMCPMC302045

What OpenQuestion holds

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Registered trials

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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.