Evidence map›Paper›PMID 38418607›Full record

ArticlePlant cell reports2024

Cathepsin B degrades RbcL during freezing-induced programmed cell death in Arabidopsis.

Gang Yang, Tao Chen, Ting-Ting Fan, Xiang-Yu Lin, Yu-Qiong Cui, Wei-Chao Dong, Li-Zhe An, Hua Zhang

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Article in Plant cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 99% 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

2 citing papers in PubMed, 0 citations in OpenAlex.

  1. Article
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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

8 authors at 3 institutions in 1 country.

Gang YangKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.ORCID http://orcid.org/0000-0002-1637-5662
Tao ChenCollege of Life Science and Technology, Gansu Agricultural University, Lanzhou, 730070, China.
Ting-Ting FanKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
Xiang-Yu LinKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
Yu-Qiong CuiKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
Wei-Chao DongKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
Li-Zhe AnKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China. lizhean@lzu.edu.cn.
Hua ZhangKey Laboratory of Cell Activities and Stress Adaptations, Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou, 730000, China. zhanghua@lzu.edu.cn.
Lanzhou University · CNGansu Agricultural University · CNBeijing Forestry University · CN

Funding

the Key Program of the National Natural Science Foundation of China 41830321the National Natural Science Foundation of China 31770432the National Science and Technology Major Project in Gansu 17ZD2WA017
6 · The paper itself

Abstract

key messageCathepsin B plays an important role that degrades the Rubisco large subunit RbcL in freezing stress. Programmed cell death (PCD) has been well documented in both development and in response to environmental stresses in plants, however, PCD induced by freezing stress and its molecular mechanisms remain poorly understood. In the present study, we characterized freezing-induced PCD and explored its mechanisms in Arabidopsis. PCD induced by freezing stress was similar to that induced by other stresses and senescence in Arabidopsis plants with cold acclimation. Inhibitor treatment assays and immunoblotting indicated that cathepsin B mainly contributed to increased caspase-3-like activity during freezing-induced PCD. Cathepsin B was involved in freezing-induced PCD and degraded the large subunit, RbcL, of Rubisco. Our results demonstrate an essential regulatory mechanism of cathepsin B for Rubisco degradation in freezing-induced PCD, improving our understanding of freezing-induced cell death and nitrogen and carbohydrate remobilisation in plants.

Indexed as

ArabidopsisArabidopsis ProteinsApoptosisCathepsin BFreezingRibulose-Bisphosphate CarboxylaseArabidopsis ProteinsCathepsin BRibulose-Bisphosphate CarboxylaseCathepsin BFreezing stressProgrammed cell death (PCD)Rubisco large subunit (RbcL)

Identifiers

PMID38418607
OpenAlexW4392242439

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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.