Evidence map›Paper›PMID 32558910›Full record

ArticleNucleic acids research2020

State changes of the HORMA protein ASY1 are mediated by an interplay between its closure motif and PCH2.

Chao Yang, Bingyan Hu, Stephan Michael Portheine, Pichaporn Chuenban, Arp Schnittger

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Chao YangUniversity of Hamburg, Department of Developmental Biology, Ohnhorststr. 18, D-22609 Hamburg, Germany.
Bingyan HuUniversity of Hamburg, Department of Developmental Biology, Ohnhorststr. 18, D-22609 Hamburg, Germany.
Stephan Michael PortheineUniversity of Hamburg, Department of Developmental Biology, Ohnhorststr. 18, D-22609 Hamburg, Germany.
Pichaporn ChuenbanUniversity of Hamburg, Department of Developmental Biology, Ohnhorststr. 18, D-22609 Hamburg, Germany.
Arp SchnittgerUniversity of Hamburg, Department of Developmental Biology, Ohnhorststr. 18, D-22609 Hamburg, Germany.
Universität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HORMA domain-containing proteins (HORMADs) play an essential role in meiosis in many organisms. The meiotic HORMADs, including yeast Hop1, mouse HORMAD1 and HORMAD2, and Arabidopsis ASY1, assemble along chromosomes at early prophase and the closure motif at their C-termini has been hypothesized to be instrumental for this step by promoting HORMAD oligomerization. In late prophase, ASY1 and its homologs are progressively removed from synapsed chromosomes promoting chromosome synapsis and recombination. The conserved AAA+ ATPase PCH2/TRIP13 has been intensively studied for its role in removing HORMADs from synapsed chromosomes. In contrast, not much is known about how HORMADs are loaded onto chromosomes. Here, we reveal that the PCH2-mediated dissociation of the HORMA domain of ASY1 from its closure motif is important for the nuclear targeting and subsequent chromosomal loading of ASY1. This indicates that the promotion of ASY1 to an 'unlocked' state is a prerequisite for its nuclear localization and chromosomal assembly. Likewise, we find that the closure motif is also necessary for the removal of ASY1 by PCH2 later in prophase. Our work results in a unified new model for PCH2 and HORMADs function in meiosis and suggests a mechanism to contribute to unidirectionality in meiosis.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsArabidopsisArabidopsis ProteinsCell NucleusChromosome PairingChromosomes, PlantDNA-Binding ProteinsProtein DomainsSequence DeletionAdenosine TriphosphatasesArabidopsis ProteinsASY1 protein, ArabidopsisDNA-Binding ProteinsPCH2 protein, Arabidopsis

Identifiers

PMID32558910
PMCPMC7672429
OpenAlexW3036211490

What OpenQuestion holds

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LicenceCC BY-NC
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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.