Evidence map›Paper›PMID 12242276›Full record

ArticleMolecular and cellular biology2002

Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae.

Joanna Kamińska, Beata Gajewska, Anita K Hopper, Teresa Zoładek

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

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  11. Functional dissection of a HECT ubiquitin E3 ligase.Molecular & cellular proteomics : MCP · 2008
    Article
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  15. The BAR domain proteins: molding membranes in fission, fusion, and phagy.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  16. The transduction of the nitrogen regulation signal in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  17. Article
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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 at 2 institutions in 2 countries.

Joanna KamińskaDepartment of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Beata Gajewska
Anita K Hopper
Teresa Zoładek
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLPennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rsp5p is an ubiquitin-protein ligase of Saccharomyces cerevisiae that has been implicated in numerous processes including transcription, mitochondrial inheritance, and endocytosis. Rsp5p functions at multiple steps of endocytosis, including ubiquitination of substrates and other undefined steps. We propose that one of the roles of Rsp5p in endocytosis involves maintenance and remodeling of the actin cytoskeleton. We report the following. (i) There are genetic interactions between rsp5 and several mutant genes encoding actin cytoskeletal proteins. rsp5 arp2, rsp5 end3, and rsp5 sla2 double mutants all show synthetic growth defects. Overexpressed wild-type RSP5 or mutant rsp5 genes with lesions of some WW domains suppress growth defects of arp2 and end3 cells. The defects in endocytosis, actin cytoskeleton, and morphology of arp2 are also suppressed. (ii) Rsp5p and Sla2p colocalize in abnormal F-actin-containing clumps in arp2 and pan1 mutants. Immunoprecipitation experiments confirmed that Rsp5p and Act1p colocalize in pan1 mutants. (iii) Rsp5p and Sla2p coimmunoprecipitate and partially colocalize to punctate structures in wild-type cells. These studies provide the first evidence for an interaction of an actin cytoskeleton protein with Rsp5p. (iv) rsp5-w1 mutants are resistant to latrunculin A, a drug that sequesters actin monomers and depolymerizes actin filaments, consistent with the fact that Rsp5p is involved in actin cytoskeleton dynamics.

Indexed as

Saccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCytoskeletal ProteinsCytoskeletonEndocytosisEndosomal Sorting Complexes Required for TransportFungal ProteinsGenetic VectorsLigasesMutagenesisSaccharomyces cerevisiaeSubcellular FractionsThiazolesActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCytoskeletal ProteinsEndosomal Sorting Complexes Required for TransportFungal Proteinslatrunculin ALigasesRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiaeThiazolesThiazolidinesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID12242276
PMCPMC139796
OpenAlexW2130020940

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.