Evidence map›Paper›PMID 20610386›Full record

ArticleThe Journal of biological chemistry2010

Localization of myosin 1b to actin protrusions requires phosphoinositide binding.

Shigeru Komaba, Lynne M Coluccio

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  12. Myosin 1b is an actin depolymerase.Nature communications · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  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

2 authors.

Shigeru KomabaBoston Biomedical Research Institute, Watertown, Massachusetts 02472, USA.
Lynne M Coluccio

Funding

Role of myosin 1c in adaptation in the inner earR01DC008793 · NIDCD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COLUCCIO, LYNNE M · 2008 to 2012
$3.9M
Role of myosin 1c in adaptation in the inner earR55DC008793 · NIDCD · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI COLUCCIO, LYNNE M · 2007 to 2007
$100k
NIDCD NIH HHS DC08793-01NIDCD NIH HHS DC08793-01S1NIDCD NIH HHS R01 DC008793NIDCD NIH HHS R55 DC008793
6 · The paper itself

Abstract

Myosin 1b (Myo1b), a class I myosin, is a widely expressed, single-headed, actin-associated molecular motor. Transient kinetic and single-molecule studies indicate that it is kinetically slow and responds to tension. Localization and subcellular fractionation studies indicate that Myo1b associates with the plasma membrane and certain subcellular organelles such as endosomes and lysosomes. Whether Myo1b directly associates with membranes is unknown. We demonstrate here that full-length rat Myo1b binds specifically and with high affinity to phosphatidylinositol 4,5-bisphosphate (PIP(2)) and phosphatidylinositol 3,4,5-triphosphate (PIP(3)), two phosphoinositides that play important roles in cell signaling. Binding is not Ca(2+)-dependent and does not involve the calmodulin-binding IQ region in the neck domain of Myo1b. Furthermore, the binding site is contained entirely within the C-terminal tail region, which contains a putative pleckstrin homology domain. Single mutations in the putative pleckstrin homology domain abolish binding of the tail domain of Myo1b to PIP(2) and PIP(3) in vitro. These same mutations alter the distribution of Myc-tagged Myo1b at membrane protrusions in HeLa cells where PIP(2) localizes. In addition, we found that motor activity is required for Myo1b localization in filopodia. These results suggest that binding of Myo1b to phosphoinositides plays an important role in vivo by regulating localization to actin-enriched membrane projections.

Indexed as

ActinsAmino Acid SequenceAnimalsBinding SitesBlood ProteinsCell Surface ExtensionsChlorocebus aethiopsCOS CellsHeLa CellsHumansMolecular Sequence DataMovementMyosinsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsActinsBlood ProteinsMyosinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsPhospholipase C deltaPhosphoproteinsplatelet protein P47

Identifiers

PMID20610386
PMCPMC2934636

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.