Evidence map›Paper›PMID 12554638›Full record

ArticleThe EMBO journal2003

Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications.

Mohammed Terrak, Guanming Wu, Walter F Stafford, Renne C Lu, Roberto Dominguez

Abstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulatory Light Chains in Cardiac Development and Disease.International journal of molecular sciences · 2021
    Review
  4. Article
  5. Article
  6. Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Structure of androcam supports specialized interactions with myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

5 authors at 1 institution in 1 country.

Mohammed TerrakBoston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
Guanming Wu
Walter F Stafford
Renne C Lu
Roberto Dominguez
Boston Biomedical Research Institute · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
ATOMIC STRUCTURE OF SMOOTH MUSCLE CALDESMONR01AR046524 · NIAMS · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI DOMINGUEZ, ROBERTO · 2000 to 2004
$2.0M
NCRR NIH HHS P41 RR001646NCRR NIH HHS P41 RR007707NCRR NIH HHS RR-01646NCRR NIH HHS RR07707NIAMS NIH HHS R01 AR046524NIAMS NIH HHS R01 AR46524
6 · The paper itself

Abstract

IQ motifs are widespread in nature. Mlc1p is a calmodulin-like myosin light chain that binds to IQ motifs of a class V myosin, Myo2p, and an IQGAP-related protein, Iqg1p, playing a role in polarized growth and cytokinesis in Saccharomyces cerevisiae. The crystal structures of Mlc1p bound to IQ2 and IQ4 of Myo2p differ dramatically. When bound to IQ2, Mlc1p adopts a compact conformation in which both the N- and C-lobes interact with the IQ motif. However, in the complex with IQ4, the N-lobe no longer interacts with the IQ motif, resulting in an extended conformation of Mlc1p. The two light chain structures relate to two distinct subfamilies of IQ motifs, one of which does not interact with the N-lobes of calmodulin-like light chains. The correlation between light chain structure and IQ sequence is demonstrated further by sedimentation velocity analysis of complexes of Mlc1p with IQ motifs from Myo2p and Iqg1p. The resulting 'free' N-lobes of myosin light chains in the extended conformation could mediate the formation of ternary complexes during protein localization and/or partner recruitment.

Indexed as

Protein ConformationAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayModels, MolecularMolecular Sequence DataMyosin Heavy ChainsMyosin Light ChainsMyosin Type VProtein BindingSaccharomyces cerevisiae ProteinsSequence AlignmentMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Light ChainsMyosin Type VSaccharomyces cerevisiae Proteins

Identifiers

PMID12554638
PMCPMC140742
OpenAlexW2163922877

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.