Evidence map›Paper›PMID 11781338›Full record

ArticleThe Journal of cell biology2002

The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.

Arthur S Rovner, Patricia M Fagnant, Susan Lowey, Kathleen M Trybus

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026
    Review
  4. Article
  5. Review
  6. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Tuning of shortening speed in coleoid cephalopod muscle: no evidence for tissue-specific muscle myosin heavy chain isoforms.Invertebrate biology : a quarterly journal of the American Microscopical Society and the Division of Invertebrate Zoology/ASZ · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Ablation of smooth muscle myosin heavy chain SM2 increases smooth muscle contraction and results in postnatal death in mice.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  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

4 authors at 1 institution in 1 country.

Arthur S RovnerDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA. rovner@physiology.med.uvm.edu
Patricia M Fagnant
Susan Lowey
Kathleen M Trybus
University of Vermont · US

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
MOLECULAR MECHANICS OF MUTANT SMOOTH MUSCLE MYOSINSR01HL054568 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1996 to 2000
$691k
CHEMISTRY OF MUSCLE PROTEINSR01AR017350 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LOWEY, SUSAN · 1996 to 2000
$438k
CHEMISTRY OF MUSCLE PROTEINSR37AR017350 · NIAMS · BRANDEIS UNIVERSITY · PI LOWEY, SUSAN · 1986 to 1995
–
NHLBI NIH HHS HL38813NHLBI NIH HHS HL54568NHLBI NIH HHS R01 HL038113NIAMS NIH HHS AR17350
6 · The paper itself

Abstract

The alternatively spliced SM1 and SM2 smooth muscle myosin heavy chains differ at their respective carboxyl termini by 43 versus 9 unique amino acids. To determine whether these tailpieces affect filament assembly, SM1 and SM2 myosins, the rod region of these myosin isoforms, and a rod with no tailpiece (tailless), were expressed in Sf 9 cells. Paracrystals formed from SM1 and SM2 rod fragments showed different modes of molecular packing, indicating that the tailpieces can influence filament structure. The SM2 rod was less able to assemble into stable filaments than either SM1 or the tailless rods. Expressed full-length SM1 and SM2 myosins showed solubility differences comparable to the rods, establishing the validity of the latter as a model for filament assembly. Formation of homodimers of SM1 and SM2 rods was favored over the heterodimer in cells coinfected with both viruses, compared with mixtures of the two heavy chains renatured in vitro. These results demonstrate for the first time that the smooth muscle myosin tailpieces differentially affect filament assembly, and suggest that homogeneous thick filaments containing SM1 or SM2 myosin could serve distinct functions within smooth muscle cells.

Indexed as

Actin CytoskeletonAlternative SplicingAmino Acid SequenceAnimalsChickensCrystallizationDimerizationGizzard, AvianMicroscopy, ElectronMolecular Sequence DataMyosin Heavy ChainsProtein IsoformsProtein Structure, QuaternaryRabbitsRatsRecombinant ProteinsMyosin Heavy ChainsProtein IsoformsRecombinant ProteinsSmooth Muscle Myosins

Identifiers

PMID11781338
PMCPMC2173570
OpenAlexW2152224598

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.