Evidence map›Paper›PMID 39569378›Full record

ArticleiScience2024

Modulation of stress granule dynamics by phosphorylation and ubiquitination in plants.

Siou-Luan He, Xiling Wang, Sung-Il Kim, Liang Kong, Ailing Liu, Lei Wang, Ying Wang, Libo Shan, Ping He, Jyan-Chyun Jang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
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

10 authors.

Siou-Luan HeDepartment of Horticulture and Crop Science, Center for Applied Plant Sciences, and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Xiling WangKey Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, and University of Chinese Academy of Sciences, Beijing 10093, China.
Sung-Il KimDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1085, USA.
Liang KongDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1085, USA.
Ailing LiuDepartment of Horticulture and Crop Science, Center for Applied Plant Sciences, and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Lei WangKey Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, and University of Chinese Academy of Sciences, Beijing 10093, China.
Ying WangPlant Pathology Department and Plant Molecular Cellular Biology Program, University of Florida, Gainesville, FL 32611, USA.
Libo ShanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1085, USA.
Ping HeDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1085, USA.
Jyan-Chyun JangDepartment of Horticulture and Crop Science, Center for Applied Plant Sciences, and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arabidopsis tandem CCCH zinc finger 1 (TZF1) is an RNA-binding protein that plays a pivotal role in plant growth and stress response. In this report, we show that TZF1 contains two intrinsically disordered regions necessary for its localization to stress granules (SGs). TZF1 recruits mitogen-activated protein kinase (MAPK) signaling components and an E3 ubiquitin ligase KEEP-ON-GOING (KEG) to SGs. TZF1 is phosphorylated by MPKs and ubiquitinated by KEG. Using a high throughput Arabidopsis protoplasts transient expression system, mutant studies reveal that the phosphorylation of specific residues plays differential roles in enhancing or reducing TZF1 SG assembly and protein-protein interaction with mitogen-activated kinase kinase 5 in SGs. Ubiquitination appears to play a positive role in TZF1 SG assembly, because mutations cause a reduction of typical SGs, while enhancing the assembly of large SGs encompassing the nucleus. Together, our results demonstrate that plant SG assembly is distinctively regulated by phosphorylation and ubiquitination.

Indexed as

Molecular biologyPlant BiologyPlant physiology

Identifiers

PMID39569378
PMCPMC11576400

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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.