Evidence map›Paper›PMID 30601698›Full record

ArticleMolecular biology of the cell2019

Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes.

Yage Zhang, Fakun Cao, Yuhuan Zhou, Zhen Feng, Brian Sit, Mira Krendel, Cheng-Han Yu

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  9. Review
  10. Article
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  12. Article
  13. PI(3,4)PProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Article
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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

7 authors at 3 institutions in 3 countries.

Yage ZhangSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
Fakun CaoSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
Yuhuan ZhouSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
Zhen FengSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
Brian SitSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
Mira KrendelSUNY Upstate Medical University, Syracuse, NY 13210.
Cheng-Han YuSchool of Biomedical Sciences, Faculty of Medicine, University of Hong Kong, Hong Kong.
University of Hong Kong · HKKing's College London · GBSUNY Upstate Medical University · US

Funding

Role of myosin 1e in podocyte biology and renal filtrationR01DK083345 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI Mira Krendel · 2011 to 2026
$6.8M
NIDDK NIH HHS R01 DK083345
6 · The paper itself

Abstract

During podosome formation, distinct phosphatidylinositol 3,4,5-trisphosphate lipid (PI(3,4,5)P3) production and F-actin polymerization take place at integrin-mediated adhesions. Membrane-associated actin regulation factors, such as myosin-1, serve as key molecules to link phosphatidylinositol signals to podosome assembly. Here, we report that long-tailed myosin-1e (Myo1e) is enriched at the ventral layer of the podosome core in a PI(3,4,5)P3-dependent manner. The combination of TH1 and TH2 (TH12) of Myo1e tail domains contains the essential motif for PI(3,4,5)P3-dependent membrane association and ventral localization at the podosome. TH12 KR2A (K772A and R782A) becomes dissociated from the plasma membrane. While F-actin polymerizations are initialized from the ventral layer of the podosome, TH12 precedes the recruitment of N-WASP and Arp2/3 in the initial phase of podosome formation. Overexpression of TH12, not TH12 KR2A, impedes PI(3,4,5)P3 signaling, restrains F-actin polymerization, and inhibits podosome formation. TH12 also suppresses gelatin degradation and migration speed of invadopodia-forming A375 melanoma cells. Thus, TH12 domain of Myo1e serves as a regulatory component to connect phosphatidylinositol signaling to F-actin polymerization at the podosome.

Indexed as

PolymerizationSignal TransductionActinsAnimalsCell Line, TumorCell MembraneGelatinHumansMiceMyosinsPhosphatidylinositol PhosphatesPhosphatidylinositolsPodosomesProtein BindingProtein DomainsRatsActinsGelatinMyosinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesPhosphatidylinositols

Identifiers

PMID30601698
PMCPMC6589698
OpenAlexW2906763177

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.