Evidence map›Paper›PMID 10397764›Full record

ArticleMolecular biology of the cell1999

Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals.

S Yang, M J Cope, D G Drubin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.9field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Raynals, an online tool for the analysis of dynamic light scattering.Acta crystallographica. Section D, Structural biology · 2023
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  7. Integrins in disguise - mechanosensors inMicrobial cell (Graz, Austria) · 2019
    Review
  8. Article
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  13. Review
  14. Molecular basis for coupling the plasma membrane to the actin cytoskeleton during clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Article
  16. Review
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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

3 authors at 1 institution in 1 country.

S YangDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202, USA.
M J Cope
D G Drubin
Baylor College of Medicine · US

Funding

The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
NIGMS NIH HHS GM-50399NIGMS NIH HHS R01 GM050399
6 · The paper itself

Abstract

Sla2p, also known as End4p and Mop2p, is the founding member of a widely conserved family of actin-binding proteins, a distinguishing feature of which is a C-terminal region homologous to the C terminus of talin. These proteins may function in actin cytoskeleton-mediated plasma membrane remodeling. A human homologue of Sla2p binds to huntingtin, the protein whose mutation results in Huntington's disease. Here we establish by immunolocalization that Sla2p is a component of the yeast cortical actin cytoskeleton. Deletion analysis showed that Sla2p contains two separable regions, which can mediate association with the cortical actin cytoskeleton, and which can provide Sla2p function. One localization signal is actin based, whereas the other signal is independent of filamentous actin. Biochemical analysis showed that Sla2p exists as a dimer in vivo. Two-hybrid analysis revealed two intramolecular interactions mediated by coiled-coil domains. One of these interactions appears to underlie dimer formation. The other appears to contribute to the regulation of Sla2p distribution between the cytoplasm and plasma membrane. The data presented are used to develop a model for Sla2p regulation and interactions.

Indexed as

Saccharomyces cerevisiae ProteinsActinsBase SequenceCarrier ProteinsCell DivisionCytoskeletal ProteinsCytoskeletonDimerizationDNA-Binding ProteinsEndocytosisFungal ProteinsGene DeletionMolecular Sequence DataMutationRecombinant ProteinsSignal TransductionActinsCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsFungal ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiae

Identifiers

PMID10397764
PMCPMC25442
OpenAlexW2153843294

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.