Evidence map›Paper›PMID 17994197›Full record

ArticleJournal of muscle research and cell motility2007

CIB1 and CaBP1 bind to the myo1c regulatory domain.

Nanyun Tang, Tianming Lin, Jun Yang, J Kevin Foskett, E Michael Ostap

Open access · greenAbstract read
In one paragraph

Article in Journal of muscle research and cell motility, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Putting the brakes on a myosin motor.The Journal of biological chemistry · 2020
    Article
  2. Article
  3. Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019
    Review
  4. Review
  5. CIB1: a small protein with big ambitions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Review
  6. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.Investigative ophthalmology & visual science · 2011
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Kinetics of the interaction of myo1c with phosphoinositides.The Journal of biological chemistry · 2009
    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.

Nanyun TangThe Pennsylvania Muscle Institute, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, Philadelphia, PA, 19104-6085, USA.
Tianming Lin
Jun Yang
J Kevin Foskett
E Michael Ostap
University of Pennsylvania · US

Funding

Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Electrophysiology of nuclear membrane InsP3 receptorR37GM056328 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI FOSKETT, JAMES KEVIN · 2011 to 2020
$4.9M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
ELECTROPHYSIOLOGY OF NUCLEAR MEMBRANE INSP3 RECEPTORR01GM056328 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI FOSKETT, JAMES KEVIN · 1999 to 2010
$4.2M
NIGMS NIH HHS GM56328NIGMS NIH HHS GM57247NIGMS NIH HHS R01 GM056328NIGMS NIH HHS R37 GM056328NIGMS NIH HHS R37 GM057247
6 · The paper itself

Abstract

Myo1c is a member of the myosin-I family that binds phosphoinositides and links the actin cytoskeleton to cellular membranes. Recent investigations suggest that targeting of myo1c to some subcellular regions requires the binding of an unknown protein to the IQ motifs in the myo1c regulatory domain. We identify two myristoylated proteins that bind the myo1c regulatory domain: calcium-binding protein 1 (CaBP1) and calcium- and integrin-binding-protein-1 (CIB1). CIB1 and CaBP1 interact with myo1c in vivo as determined by pull-down experiments and fluorescence microscopy where the endogenously expressed proteins show extensive cellular colocalization with myo1c. CIB1 and CaBP1 bind to the myo1c IQ motifs in the regulatory domain where they compete with calmodulin for binding. CaBP1 has a higher apparent affinity for myo1c than CIB1, and both proteins better compete with calmodulin in the presence of calcium. We propose that these proteins may play a role in specifying subcellular localization of myo1c.

Indexed as

Amino Acid MotifsAnimalsCalcium-Binding ProteinsCalmodulinChlorocebus aethiopsCOS CellsMiceMyosin Type IPC12 CellsProtein Structure, Tertiaryras GTPase-Activating ProteinsRatsCa2+-binding protein-1Calcium-Binding ProteinsCalmodulinCib1 protein, ratMyo1c protein, ratMyosin Type Iras GTPase-Activating Proteins

Identifiers

PMID17994197
PMCPMC2901637
OpenAlexW2076542505

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.