Evidence map›Paper›PMID 33514914›Full record

ArticleCell research2021

The noncanonical role of the protease cathepsin D as a cofilin phosphatase.

Yi-Jun Liu, Ting Zhang, Sicong Chen, Daxiao Cheng, Cunjin Wu, Xingyue Wang, Duo Duan, Liya Zhu, Huifang Lou, Zhefeng Gong and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023
    Pooled it
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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

13 authors at 5 institutions in 2 countries.

Yi-Jun Liu *Department of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China. yjliu@zju.edu.cn.
Ting Zhang *Department of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Sicong ChenClinical Research Center, The Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Daxiao ChengDepartment of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Cunjin WuResearch Units for Emotion and Emotion Disorders, NHC and CAMS Key Laboratory of Medical Neurobiology, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, School of Brain Science and Brain Medicine, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Xingyue WangDepartment of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Duo DuanResearch Units for Emotion and Emotion Disorders, NHC and CAMS Key Laboratory of Medical Neurobiology, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, School of Brain Science and Brain Medicine, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Liya ZhuDepartment of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Huifang LouDepartment of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.
Zhefeng GongResearch Units for Emotion and Emotion Disorders, NHC and CAMS Key Laboratory of Medical Neurobiology, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, School of Brain Science and Brain Medicine, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Xiao-Dong WangResearch Units for Emotion and Emotion Disorders, NHC and CAMS Key Laboratory of Medical Neurobiology, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, School of Brain Science and Brain Medicine, Zhejiang University, Hangzhou, Zhejiang, 310058, China. xiaodongwang@zju.edu.cn.ORCID http://orcid.org/0000-0001-7730-3710
Margaret S HoSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China. margareth@shanghaitech.edu.cn.
Shumin DuanDepartment of Neurobiology and Department of Neurology of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310009, China.ORCID http://orcid.org/0000-0002-0466-1821
Second Affiliated Hospital of Zhejiang University · CNZhejiang University · CNSir Run Run Shaw Hospital · CNEmotional Brain (Netherlands) · NLShanghaiTech University · CN

Funding

Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology) 2016YFA0501000National Natural Science Foundation of China (National Science Foundation of China) 31501128National Natural Science Foundation of China (National Science Foundation of China) 81761138044, 81971260National Natural Science Foundation of China (National Science Foundation of China) 81801330
6 · The paper itself

Abstract

Cathepsin D (cathD) is traditionally regarded as a lysosomal protease that degrades substrates in acidic compartments. Here we report cathD plays an unconventional role as a cofilin phosphatase orchestrating actin remodeling. In neutral pH environments, the cathD precursor directly dephosphorylates and activates the actin-severing protein cofilin independent of its proteolytic activity, whereas mature cathD degrades cofilin in acidic pH conditions. During development, cathD complements the canonical cofilin phosphatase slingshot and regulates the morphogenesis of actin-based structures. Moreover, suppression of cathD phosphatase activity leads to defective actin organization and cytokinesis failure. Our findings identify cathD as a dual-function molecule, whose functional switch is regulated by environmental pH and its maturation state, and reveal a novel regulatory role of cathD in actin-based cellular processes.

Indexed as

Actin Depolymerizing FactorsCathepsin DActinsCofilin 1Peptide HydrolasesPhosphoric Monoester HydrolasesActin Depolymerizing FactorsActinsCathepsin DCofilin 1Peptide HydrolasesPhosphoric Monoester Hydrolases

Identifiers

PMID33514914
PMCPMC8249557
OpenAlexW3123041035

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.