Evidence map›Paper›PMID 32503980›Full record

ArticleNature communications2020

Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.

Peng Zheng, Tu Anh Nguyen, Jie Yun Wong, Michelle Lee, The-Anh Nguyen, Jing-Song Fan, Daiwen Yang, Gregory Jedd

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

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  5. The mRNA stability factor Khd4 defines a specific mRNA regulon for membrane trafficking in the pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
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  15. Orchestrated actin nucleation by theThe Journal of biological chemistry · 2020
    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

8 authors at 2 institutions in 1 country.

Peng ZhengTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore.
Tu Anh NguyenTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore.ORCID http://orcid.org/0000-0002-9911-2402
Jie Yun WongTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore.
Michelle LeeTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore.
The-Anh NguyenTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore.
Jing-Song FanDepartment of Biological Sciences, National University of Singapore, 16 Science Drive 4, Singapore, 117558, Singapore.
Daiwen YangDepartment of Biological Sciences, National University of Singapore, 16 Science Drive 4, Singapore, 117558, Singapore.
Gregory JeddTemasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore. gregory@tll.org.sg.
Temasek Life Sciences Laboratory · SGNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Spitzenkörper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence.

Indexed as

Cell PolarityFungal ProteinsHyphaeMyosin Type VNeurospora crassaNuclear Magnetic Resonance, BiomolecularProtein DomainsProtein Interaction MapsSecretory VesiclesFungal ProteinsMyosin Type V

Identifiers

PMID32503980
PMCPMC7275032
OpenAlexW3034004098

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.