Evidence map›Paper›PMID 17928407›Full record

ArticleMolecular biology of the cell2007

The phosphorylation of myosin II at the Ser1 and Ser2 is critical for normal platelet-derived growth factor induced reorganization of myosin filaments.

Satoshi Komatsu, Mitsuo Ikebe

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  2. Article
  3. Article
  4. Targeting cytoskeletal phosphorylation in cancer.Exploration of targeted anti-tumor therapy · 2021
    Review
  5. Review
  6. Review
  7. Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Diacylglycerol promotes centrosome polarization in T cells via reciprocal localization of dynein and myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Nonmuscle myosin-2: mix and match.Cellular and molecular life sciences : CMLS · 2013
    Review
  17. Article
  18. Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Satoshi KomatsuDepartment of Physiology, University of Massachusetts Medical School, Worcester, MA 01655, USA. satoshi.komatsu@umassmed.edu
Mitsuo Ikebe
University of Massachusetts Chan Medical School · US

Funding

Regulation of Myosin Phosphorylation in Smooth MuscleR01HL073050 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2013
$4.0M
Regulation of Mammalian Class VI MyosinR01AR048526 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
MOLECULAR REGULATION OF SMOOTH MUSCLE ACTOMYOSINR01AR041653 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 1992 to 2004
$1.8M
Function of Small G-Protein Binding MyosinR01AR048898 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Motor Function and Regulation of Myosin VIIR01DC006103 · NIDCD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.5M
NHLBI NIH HHS HL073050NHLBI NIH HHS R01 HL073050NIAMS NIH HHS AR048526NIAMS NIH HHS AR048898NIAMS NIH HHS AR41653NIAMS NIH HHS R01 AR041653NIAMS NIH HHS R01 AR048526NIAMS NIH HHS R01 AR048898NIDCD NIH HHS DC006103NIDCD NIH HHS R01 DC006103
6 · The paper itself

Abstract

Phosphorylation of the regulatory light chain of myosin II (MLC(20)) at the activation sites promotes both the motor activity and the filament formation of myosin II, thus playing an important role in various cell motile processes. In contrast, the physiological function of phosphorylation of MLC(20) at the inhibitory sites is unknown. Here we report for the first time the function of the inhibitory site phosphorylation in the cells. We successfully produced the antibodies specifically recognizing the phosphorylation sites of MLC(20) at Ser1, and the platelet-derived growth factor (PDGF)-induced change in the phosphorylation at the Ser1 was monitored. The phosphorylation of MLC(20) at the Ser1 significantly increased during the PDGF-induced actin cytoskeletal reorganization. PDGF disassembled the stress fibers, and this was attenuated with the expression of unphosphorylatable MLC(20) at the Ser1/Ser2 phosphorylation sites. The present results suggest that the down-regulation of myosin II activity achieved by the phosphorylation at the Ser1/Ser2 sites plays an important role in the normal reorganization of actomyosin filaments triggered by PDGF receptor stimulation.

Indexed as

AnimalsAntibodiesMiceMyosin Type IINIH 3T3 CellsPhosphorylationPhosphoserinePlatelet-Derived Growth FactorProtein Kinase CProtein Kinase InhibitorsReceptors, Platelet-Derived Growth FactorSensitivity and SpecificityAntibodiesMyosin Type IIPhosphoserinePlatelet-Derived Growth FactorProtein Kinase CProtein Kinase InhibitorsReceptors, Platelet-Derived Growth Factor

Identifiers

PMID17928407
PMCPMC2096596
OpenAlexW2147509121

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.