Evidence map›Paper›PMID 17910470›Full record

ArticleBiochemistry2007

Calcium regulation of calmodulin binding to and dissociation from the myo1c regulatory domain.

Slobodanka Manceva, Tianming Lin, Huy Pham, John H Lewis, Yale E Goldman, E Michael Ostap

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Putting the brakes on a myosin motor.The Journal of biological chemistry · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  15. Various Themes of Myosin Regulation.Journal of molecular biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors at 1 institution in 1 country.

Slobodanka MancevaThe Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, B400 Richards Building, Philadelphia, Pennsylvania 19104-6085, USA.
Tianming Lin
Huy Pham
John H Lewis
Yale E Goldman
E Michael Ostap
University of Pennsylvania · US

Funding

Regulation and Mechano-Chemistry of Myosins V and VIP01AR051174 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2004 to 2008
$7.1M
Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Training in Muscle Biology and Muscle DiseaseT32AR053461 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2006 to 2025
$4.9M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
NIAMS NIH HHS AR051174NIAMS NIH HHS AR053461NIAMS NIH HHS P01 AR051174NIAMS NIH HHS T32 AR053461NIGMS NIH HHS GM57247NIGMS NIH HHS R01 GM057247
6 · The paper itself

Abstract

Myo1c is an unconventional myosin involved in cell signaling and membrane dynamics. Calcium binding to the regulatory-domain-associated calmodulin affects myo1c motor properties, but the kinetic details of this regulation are not fully understood. We performed actin gliding assays, ATPase measurements, fluorescence spectroscopy, and stopped-flow kinetics to determine the biochemical parameters that define the calmodulin-regulatory-domain interaction. We found calcium moderately increases the actin-activated ATPase activity and completely inhibits actin gliding. Addition of exogenous calmodulin in the presence of calcium fully restores the actin gliding rate. A fluorescently labeled calmodulin mutant (N111C) binds to recombinant peptides containing the myo1c IQ motifs at a diffusion-limited rate in the presence and absence of calcium. Measurements of calmodulin dissociation from the IQ motifs in the absence of calcium show that the calmodulin bound to the IQ motif adjacent to the motor domain (IQ1) has the slowest dissociation rate (0.0007 s-1), and the IQ motif adjacent to the tail domain (IQ3) has the fastest dissociation rate (0.5 s-1). When the complex is equilibrated with calcium, calmodulin dissociates most rapidly from IQ1 (60 s-1). However, this increased rate of dissociation is limited by a slow calcium-induced conformational change (3 s-1). Fluorescence anisotropy decay of fluorescently labeled N111C bound to myo1c did not depend appreciably on Ca2+. Our data suggest that the calmodulin bound to the IQ motif adjacent to the motor domain is rapidly exchangeable in the presence of calcium and is responsible for regulation of myo1c ATPase and motile activity.

Indexed as

ActinsAdenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesBiotinylationCalciumCalmodulinChickensConsensus SequenceDiffusionDose-Response Relationship, DrugEgtazic AcidFluorescence PolarizationKineticsActinsAdenosine TriphosphatasesCalciumCalmodulinEgtazic AcidMyosin Type IPeptidesRecombinant Proteins

Identifiers

PMID17910470
PMCPMC2566900
OpenAlexW1970331854

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.