Evidence map›Paper›PMID 25637593›Full record

ArticleJournal of cell science2015

Actin depolymerisation and crosslinking join forces with myosin II to contract actin coats on fused secretory vesicles.

Pika Miklavc, Konstantin Ehinger, Ayesha Sultan, Tatiana Felder, Patrick Paul, Kay-Eberhard Gottschalk, Manfred Frick

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. P2 Purinergic Signaling in the Distal Lung in Health and Disease.International journal of molecular sciences · 2020
    Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. ATP is stored in lamellar bodies to activate vesicular P2XThe Journal of general physiology · 2018
    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

7 authors at 1 institution in 1 country.

Pika MiklavcDepartment of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Konstantin EhingerDepartment of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Ayesha SultanDepartment of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Tatiana FelderDepartment of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Patrick PaulInstitute for Experimental Physics, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Kay-Eberhard GottschalkInstitute for Experimental Physics, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Manfred FrickDepartment of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany manfred.frick@uni-ulm.de.
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In many secretory cells actin and myosin are specifically recruited to the surface of secretory granules following their fusion with the plasma membrane. Actomyosin-dependent compression of fused granules is essential to promote active extrusion of cargo. However, little is known about molecular mechanisms regulating actin coat formation and contraction. Here, we provide a detailed kinetic analysis of the molecules regulating actin coat contraction on fused lamellar bodies in primary alveolar type II cells. We demonstrate that ROCK1 and myosin light chain kinase 1 (MLCK1, also known as MYLK) translocate to fused lamellar bodies and activate myosin II on actin coats. However, myosin II activity is not sufficient for efficient actin coat contraction. In addition, cofilin-1 and α-actinin translocate to actin coats. ROCK1-dependent regulated actin depolymerisation by cofilin-1 in cooperation with actin crosslinking by α-actinin is essential for complete coat contraction. In summary, our data suggest a complementary role for regulated actin depolymerisation and crosslinking, and myosin II activity, to contract actin coats and drive secretion.

Indexed as

Actin CytoskeletonActininActinsAnimalsBlotting, WesternCells, CulturedExocytosisFluorescent Antibody TechniqueMembrane FusionMyosin-Light-Chain KinaseMyosin Type IIPhosphorylationRatsRats, Sprague-DawleyReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionActininActinsMyosin-Light-Chain KinaseMyosin Type IIrho-Associated Kinasesrho GTP-Binding ProteinsRNA, MessengerROCK1 protein, ratCofilinLamellar bodyMLCKROCKSecretionSurfactant

Identifiers

PMID25637593
PMCPMC4359923
OpenAlexW2104171657

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.