Evidence map›Paper›PMID 16971510›Full record

ArticleMolecular biology of the cell2006

Myo1c binds phosphoinositides through a putative pleckstrin homology domain.

David E Hokanson, Joseph M Laakso, Tianming Lin, David Sept, E Michael Ostap

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

97 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. ATP8B1 regulates PIP2 localization and cleavage of pyroptotic executioner Gasdermin D.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Interplay between mechanics and signalling in regulating cell fate.Nature reviews. Molecular cell biology · 2022
    Review
  16. An update on genetically encoded lipid biosensors.Molecular biology of the cell · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021
    Review

37 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

5 authors at 2 institutions in 1 country.

David E HokansonThe Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085, USA.
Joseph M Laakso
Tianming Lin
David Sept
E Michael Ostap
University of Pennsylvania · USWashington University in St. Louis · US

Funding

Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NIGMS NIH HHS GM-067246NIGMS NIH HHS GM-57247NIGMS NIH HHS R01 GM057247NIGMS NIH HHS R01 GM067246NIGMS NIH HHS R37 GM057247
6 · The paper itself

Abstract

Myo1c is a member of the myosin superfamily that binds phosphatidylinositol-4,5-bisphosphate (PIP(2)), links the actin cytoskeleton to cellular membranes and plays roles in mechano-signal transduction and membrane trafficking. We located and characterized two distinct membrane binding sites within the regulatory and tail domains of this myosin. By sequence, secondary structure, and ab initio computational analyses, we identified a phosphoinositide binding site in the tail to be a putative pleckstrin homology (PH) domain. Point mutations of residues known to be essential for polyphosphoinositide binding in previously characterized PH domains inhibit myo1c binding to PIP(2) in vitro, disrupt in vivo membrane binding, and disrupt cellular localization. The extended sequence of this binding site is conserved within other myosin-I isoforms, suggesting they contain this putative PH domain. We also characterized a previously identified membrane binding site within the IQ motifs in the regulatory domain. This region is not phosphoinositide specific, but it binds anionic phospholipids in a calcium-dependent manner. However, this site is not essential for in vivo membrane binding.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCell SurvivalEpithelial CellsFluorescence Recovery After PhotobleachingKineticsLipid MetabolismMiceModels, MolecularMolecular Sequence DataMyosinsMyosin Type IPhosphatidylinositol PhosphatesPoint MutationProtein BindingMyo1c protein, mouseMyosinsMyosin Type IPhosphatidylinositol PhosphatesRecombinant Fusion ProteinsUnilamellar Liposomes

Identifiers

PMID16971510
PMCPMC1635404
OpenAlexW2150094144

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.