Evidence map›Paper›PMID 9159132›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals.

R O McCann, S W Craig

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
3.5field-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

75 citing papers in PubMed, 181 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Mechanical Basis of Memory - the MeshCODE Theory.Frontiers in molecular neuroscience · 2021
    Article
  10. Article
  11. Article
  12. Integrins in disguise - mechanosensors inMicrobial cell (Graz, Austria) · 2019
    Review
  13. Review
  14. Green Fluorescent Protein- andFrontiers in plant science · 2019
    Article
  15. Talin as a mechanosensitive signaling hub.The Journal of cell biology · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

15 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

2 authors at 1 institution in 1 country.

R O McCannDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
S W Craig
Johns Hopkins Medicine · US

Funding

CELL SURFACE CONTROL OF LYMPHOCYTE PHYSIOLOGYR01GM041605 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CRAIG, SUSAN W · 1988 to 2011
$3.9M
Cell Surface Control of Cellular PhysiologyR56GM041605 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CRAIG, SUSAN W · 2007 to 2007
$403k
NIGMS NIH HHS GM41605NIGMS NIH HHS R01 GM041605NIGMS NIH HHS R56 GM041605
6 · The paper itself

Abstract

Talin is an actin-binding protein involved in integrin-mediated cell adhesion and spreading. The C-terminal 197 amino acids of vertebrate talin are 45% similar to the C-terminal residues of Sla2, a yeast protein implicated in polarized assembly of the yeast actin cytoskeleton. Talin is also homologous in this region to nematode talin, cellular slime mold filopodin, and an Sla2 homolog from nematode. Analysis of the conserved C-terminal sequences of these five proteins with BLOCK MAKER reveals a series of four blocks, which we name the I/LWEQ module after the conserved initial residues in each block. Experiments presented here show that the conserved protein domain represented by the I/LWEQ module competes quantitatively with native talin for binding to F-actin in vitro. Furthermore, the corresponding domain of Sla2 binds to both yeast and vertebrate F-actin in vitro. Mutation of one of the conserved residues in the fourth conserved block abolishes the interaction of the Sla2 I/LWEQ module with F-actin. These results establish the location of an F-actin binding domain in native talin, demonstrate that direct interaction of Sla2 with actin is a possible basis for its effect on the actin cytoskeleton in vivo, and define the I/LWEQ consensus as a new actin-binding motif.

Indexed as

ActinsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansConserved SequenceDNA PrimersKineticsMammalsMiceMolecular Sequence DataMuscle, SkeletalNematodaPolymerase Chain ReactionRabbitsRecombinant Fusion ProteinsActinsDNA PrimersRecombinant Fusion ProteinsTalin

Identifiers

PMID9159132
PMCPMC20838
OpenAlexW2077232274

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.