Evidence map›Paper›PMID 14973168›Full record

ArticleThe Plant cell2004

The F-box protein AhSLF-S2 physically interacts with S-RNases that may be inhibited by the ubiquitin/26S proteasome pathway of protein degradation during compatible pollination in Antirrhinum.

Hong Qiao, Hongyun Wang, Lan Zhao, Junli Zhou, Jian Huang, Yansheng Zhang, Yongbiao Xue

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

89 citing papers in PubMed, 196 citations in OpenAlex.

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  10. Genome-Wide Analysis of theInternational journal of molecular sciences · 2022
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  16. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
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29 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

7 authors at 2 institutions in 1 country.

Hong QiaoInstitute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100080, China.
Hongyun Wang
Lan Zhao
Junli Zhou
Jian Huang
Yansheng Zhang
Yongbiao Xue
Chinese Academy of Sciences · CNInstitute of Genetics and Developmental Biology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Self-incompatibility S-locus-encoded F-box (SLF) proteins have been identified in Antirrhinum and several Prunus species. Although they appear to play an important role in self-incompatible reaction, functional evidence is lacking. Here, we provide several lines of evidence directly implicating a role of AhSLF-S(2) in self-incompatibility in Antirrhinum. First, a nonallelic physical interaction between AhSLF-S(2) and S-RNases was demonstrated by both coimmunoprecipitation and yeast two-hybrid assays. Second, AhSLF-S(2) interacts with ASK1- and CULLIN1-like proteins in Antirrhinum, and together, they likely form an Skp1/Cullin or CDC53/F-box (SCF) complex. Third, compatible pollination was specifically blocked after the treatment of the proteasomal inhibitors MG115 and MG132, but they had little effect on incompatible pollination both in vitro and in vivo, indicating that the ubiquitin/26S proteasome activity is involved in compatible pollination. Fourth, the ubiquitination level of style proteins was increased substantially after compatible pollination compared with incompatible pollination, and coimmunoprecipitation revealed that S-RNases were ubiquitinated after incubating pollen proteins with compatible but not with incompatible style proteins, suggesting that non-self S-RNases are possibly degraded by the ubiquitin/26S proteasome pathway. Fifth, the S-RNase level appeared to be reduced after 36 h of compatible pollination. Taken together, these results show that AhSLF-S(2) interacts with S-RNases likely through a proposed SCF(AhSLF-S2) complex that targets S-RNase destruction during compatible rather than incompatible pollination, thus providing a biochemical basis for the inhibition of pollen tube growth as observed in self-incompatible response in Antirrhinum.

Indexed as

Proteasome Endopeptidase ComplexAntirrhinumArabidopsis ProteinsBinding SitesCell Cycle ProteinsCullin ProteinsF-Box ProteinsFertilizationPeptide HydrolasesPlant ProteinsPollenProtease InhibitorsProtein BindingRecombinant ProteinsRibonucleasesTwo-Hybrid System TechniquesArabidopsis ProteinsASK1 protein, ArabidopsisATP dependent 26S proteaseCell Cycle ProteinsCullin 1Cullin ProteinsF-Box ProteinsPeptide HydrolasesPlant ProteinsProtease InhibitorsProteasome Endopeptidase ComplexRecombinant Proteinsribonuclease SRibonucleasesUbiquitin

Identifiers

PMID14973168
PMCPMC385274
OpenAlexW2103155613

What OpenQuestion holds

Textmetadata
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.