Evidence map›Paper›PMID 27113777›Full record

ArticleThe Plant cell2016

The SUMO E3 Ligase-Like Proteins PIAL1 and PIAL2 Interact with MOM1 and Form a Novel Complex Required for Transcriptional Silencing.

Yong-Feng Han, Qiu-Yuan Zhao, Liang-Liang Dang, Yu-Xi Luo, Shan-Shan Chen, Chang-Rong Shao, Huan-Wei Huang, Yong-Qiang Li, Lin Li, Tao Cai and 2 more

Abstract read
In one paragraph

Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Review
  2. A chromatin-linked CPL2-PHD2/3 module sustains multiple DNA methylation pathways and Polycomb silencing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. The MOM1 complex recruits the RdDM machinery via MORC6 to establishbioRxiv : the preprint server for biology · 2023
    Article
  7. TheFrontiers in plant science · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Protein sumoylation and phosphorylation intersect in Arabidopsis signaling.The Plant journal : for cell and molecular biology · 2017
    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

12 authors.

Yong-Feng HanNational Institute of Biological Sciences, Beijing 102206, China.ORCID 0000-0002-5626-668X
Qiu-Yuan ZhaoNational Institute of Biological Sciences, Beijing 102206, China Graduate School of Peking Union Medical College, Beijing 100730, China.ORCID 0000-0002-0295-3513
Liang-Liang DangNational Institute of Biological Sciences, Beijing 102206, China.
Yu-Xi LuoNational Institute of Biological Sciences, Beijing 102206, China.
Shan-Shan ChenNational Institute of Biological Sciences, Beijing 102206, China.
Chang-Rong ShaoNational Institute of Biological Sciences, Beijing 102206, China.
Huan-Wei HuangNational Institute of Biological Sciences, Beijing 102206, China.
Yong-Qiang LiNational Institute of Biological Sciences, Beijing 102206, China.
Lin LiNational Institute of Biological Sciences, Beijing 102206, China.
Tao CaiNational Institute of Biological Sciences, Beijing 102206, China.
She ChenNational Institute of Biological Sciences, Beijing 102206, China.
Xin-Jian HeNational Institute of Biological Sciences, Beijing 102206, China Graduate School of Peking Union Medical College, Beijing 100730, China hexinjian@nibs.ac.cn.ORCID 0000-0002-2878-7461

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism by which MORPHEUS' MOLECULE1 (MOM1) contributes to transcriptional gene silencing has remained elusive since the gene was first identified and characterized. Here, we report that two Arabidopsis thaliana PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins, PIAL1 and PIAL2, function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high molecular mass complex. In the absence of either PIAL2 or MOM1, the formation of the high molecular mass complex is disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2 and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has SUMO E3 ligase activity, the activity is dispensable for PIAL2's function in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

Indexed as

ArabidopsisArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesGene Expression Regulation, PlantGene SilencingNuclear ProteinsProtein BindingTranscription FactorsArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesMOM protein, ArabidopsisNuclear ProteinsTranscription Factors

Identifiers

PMID27113777
PMCPMC4904672

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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.