Evidence map›Paper›PMID 22027862›Full record

ArticleThe EMBO journal2012

Myosin-5, kinesin-1 and myosin-17 cooperate in secretion of fungal chitin synthase.

Martin Schuster, Steffi Treitschke, Sreedhar Kilaru, Justin Molloy, Nicholas J Harmer, Gero Steinberg

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Fungal Chitin Synthases: Structure, Function, and Regulation.Journal of fungi (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Chitin Biosynthesis inJournal of fungi (Basel, Switzerland) · 2023
    Review
  11. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  12. Article
  13. The MIT domain of chitin synthase 1 from the oomyceteBiochemistry and biophysics reports · 2022
    Article
  14. Article
  15. Article
  16. NADPH Oxidases Play a Role in PathogenicityFrontiers in cellular and infection microbiology · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Off the wall: The rhyme and reason ofCell surface (Amsterdam, Netherlands) · 2019
    Review

5 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Martin SchusterDepartment of Biosciences, University of Exeter, Exeter, UK.
Steffi Treitschke
Sreedhar Kilaru
Justin Molloy
Nicholas J Harmer
Gero Steinberg
University of Exeter · GBFraunhofer Institute for Toxicology and Experimental Medicine · DE

Funding

Biotechnology and Biological Sciences Research Council BB/G00465X/1Biotechnology and Biological Sciences Research Council BB/H019774/1Medical Research Council MC_U117570592
6 · The paper itself

Abstract

Plant infection by pathogenic fungi requires polarized secretion of enzymes, but little is known about the delivery pathways. Here, we investigate the secretion of cell wall-forming chitin synthases (CHSs) in the corn pathogen Ustilago maydis. We show that peripheral filamentous actin (F-actin) and central microtubules (MTs) form independent tracks for CHSs delivery and both cooperate in cell morphogenesis. The enzyme Mcs1, a CHS that contains a myosin-17 motor domain, is travelling along both MTs and F-actin. This transport is independent of kinesin-3, but mediated by kinesin-1 and myosin-5. Arriving vesicles pause beneath the plasma membrane, but only ~15% of them get exocytosed and the majority is returned to the cell centre by the motor dynein. Successful exocytosis at the cell tip and, to a lesser extent at the lateral parts of the cell requires the motor domain of Mcs1, which captures and tethers the vesicles prior to secretion. Consistently, Mcs1-bound vesicles transiently bind F-actin but show no motility in vitro. Thus, kinesin-1, myosin-5 and dynein mediate bi-directional motility, whereas myosin-17 introduces a symmetry break that allows polarized secretion.

Indexed as

Chitin SynthaseCytoskeletonFungal ProteinsKinesinsMicrotubulesMyosinsUstilagoChitin SynthaseFungal ProteinsKinesinsMyosins

Identifiers

PMID22027862
PMCPMC3252574
OpenAlexW2162382895

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.