Evidence map›Paper›PMID 12857851›Full record

ArticleMolecular biology of the cell2003

The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton.

Anya Goodman, Bruce L Goode, Paul Matsudaira, Gerald R Fink

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. 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
2.4field-weighted citation impact, top 11% 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

52 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. A role for cross-linking proteins in actin filament network organization and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Differential Expression ofFrontiers in cell and developmental biology · 2021
    Article
  13. Vascular Aging in the Invertebrate Chordate,Frontiers in molecular biosciences · 2021
    Article
  14. TwoThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 1 country.

Anya GoodmanWhitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Cambridge, Massachusetts 02142, USA.
Bruce L Goode
Paul Matsudaira
Gerald R Fink
Whitehead Institute for Biomedical Research · USBrandeis University · US

Funding

REGULATION OF HISTIDINE BIOSYNTHESIS IN YEASTR01GM035010 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI FINK, GERALD R · 1985 to 2016
$9.9M
MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
STRUCTURE/FUNCTION OF CH DOMAIN PROTEINSR01GM057418 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI MATSUDAIRA, PAUL T. · 1998 to 2005
$2.0M
REGULATION OF HISTIDINE BIOSYNTHESIS IN YEASTR37GM035010 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI FINK, GERALD R · 1986 to 1995
–
NIGMS NIH HHS GM-35010NIGMS NIH HHS GM-63691NIGMS NIH HHS GM-/AR57418NIGMS NIH HHS R01 GM035010NIGMS NIH HHS R01 GM063691
6 · The paper itself

Abstract

Calponins and transgelins are members of a conserved family of actin-associated proteins widely expressed from yeast to humans. Although a role for calponin in muscle cells has been described, the biochemical activities and in vivo functions of nonmuscle calponins and transgelins are largely unknown. Herein, we have used genetic and biochemical analyses to characterize the budding yeast member of this family, Scp1, which most closely resembles transgelin and contains one calponin homology (CH) domain. We show that Scp1 is a novel component of yeast cortical actin patches and shares in vivo functions and biochemical activities with Sac6/fimbrin, the one other actin patch component that contains CH domains. Purified Scp1 binds directly to filamentous actin, cross-links actin filaments, and stabilizes filaments against disassembly. Sequences in Scp1 sufficient for actin binding and cross-linking reside in its carboxy terminus, outside the CH domain. Overexpression of SCP1 suppresses sac6Delta defects, and deletion of SCP1 enhances sac6Delta defects. Together, these data show that Scp1 and Sac6/fimbrin cooperate to stabilize and organize the yeast actin cytoskeleton.

Indexed as

Actin CytoskeletonAmino Acid SequenceCalcium-Binding ProteinsCalponinsCytoskeletonMembrane GlycoproteinsMicrofilament ProteinsMolecular Sequence DataMuscle ProteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidCalcium-Binding ProteinsCalponinsMembrane GlycoproteinsMicrofilament ProteinsMuscle ProteinsplastinSaccharomyces cerevisiae ProteinsSCP1 protein, S cerevisiaeTagln protein, mousetransgelin

Identifiers

PMID12857851
PMCPMC165663
OpenAlexW2142838156

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.