Evidence map›Paper›PMID 38172660›Full record

ArticleBMC molecular and cell biology2024

Sumoylation of SAP130 regulates its interaction with FAF1 as well as its protein stability and transcriptional repressor function.

Chang-Han Chen, Hung-Wei Lin, Meng-Fang Huang, Chi-Wu Chiang, Kuen-Haur Lee, Nguyen Thanh Phuong, Zong-Yan Cai, Wen-Chang Chang, Ding-Yen Lin

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC molecular and cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 48% of its field
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

9 authors at 3 institutions in 1 country.

Chang-Han ChenDepartment of Medical Research, Taichung Veterans General Hospital, Taichung, 407219, Taiwan, ROC.
Hung-Wei LinDepartment of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Meng-Fang HuangDepartment of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Chi-Wu ChiangInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Kuen-Haur LeeInstitute for Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei, 11031, Taiwan, ROC.
Nguyen Thanh PhuongDepartment of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Zong-Yan CaiDepartment of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Wen-Chang ChangDepartment of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan, ROC.
Ding-Yen LinDepartment of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, 70101, Taiwan, ROC. lindy@mail.ncku.edu.tw.
National Cheng Kung University · TWTaipei Medical University · TWNational Chi Nan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFas-associated factor 1 (FAF1) is a multidomain protein that interacts with diverse partners to affect numerous cellular processes. Previously, we discovered two Small Ubiquitin-like Modifier (SUMO)-interacting motifs (SIMs) within FAF1 that are crucial for transcriptional modulation of mineralocorticoid receptor. Recently, we identified Sin3A-associated protein 130 (SAP130), a putative sumoylated protein, as a candidate FAF1 interaction partner by yeast two-hybrid screening. However, it remained unclear whether SAP130 sumoylation might occur and functionally interact with FAF1.

resultsIn this study, we first show that SAP130 can be modified by SUMO1 at Lys residues 794, 878 and 932 both in vitro and in vivo. Mutation of these three SUMO-accepting Lys residues to Ala had no impact on SAP130 association with Sin3A or its nuclear localization, but the mutations abrogated the association of SAP130 with the FAF1. The mutations also potentiated SAP130 trans-repression activity and attenuated SAP130-mediated promotion of cell growth. Additionally, SUMO1-modified SAP130 was less stable than unmodified SAP130. Transient transfection experiments further revealed that FAF1 mitigated the trans-repression and cell proliferation-promoting functions of SAP130, and promoted SAP130 degradation by enhancing its polyubiquitination in a sumoylation-dependent manner.

conclusionsTogether, these results demonstrate that sumoylation of SAP130 regulates its biological functions and that FAF1 plays a crucial role in controlling the SUMO-dependent regulation of transcriptional activity and protein stability of SAP130.

Indexed as

SumoylationTranscription FactorsProtein StabilityUbiquitinationTranscription FactorsFAF1SAP130SUMO-interacting motifs (SIMs)Sumoylation

Identifiers

PMID38172660
PMCPMC10765799
OpenAlexW4390585279

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Registered trials

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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.