Evidence map›Paper›PMID 41272290›Full record

ArticleCell death and differentiation2026

UFL1-mediated UFMylation antagonizes IFT88 ubiquitination and degradation to maintain ciliary homeostasis.

Runa Wang, Guizhi Guo, Renshuai Zhang, Lin Li, Yingxin Gong, Long Yin, Shuhua Li, Changfeng Wei, Jun Zhou, Min Liu and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death and differentiation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

11 authors.

Runa Wang *Center for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Guizhi Guo *Center for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Renshuai Zhang *Center for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.ORCID 0009-0009-3772-2959
Lin LiCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Yingxin GongCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Long YinCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Shuhua LiCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Changfeng WeiCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.
Jun ZhouCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China.ORCID 0000-0003-3131-7804
Min LiuCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China. minliu@sdnu.edu.cn.
Jie RanCenter for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, China. jran@sdnu.edu.cn.ORCID 0000-0002-0744-7126

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32170687 and 32241014Taishan Scholar Foundation of Shandong Province tsqn202408138
6 · The paper itself

Abstract

UFMylation, a post-translational modification involving the covalent conjugation of ubiquitin-fold modifier 1 (UFM1) to target proteins, has been implicated in a wide spectrum of human diseases. However, the underlying molecular mechanisms are poorly understood. Herein, we demonstrate that UFM1-specific ligase 1 (UFL1), the sole ligase for UFMylation, is indispensable for ciliary homeostasis. Genetic ablation of UFL1 in mice results in severe defects in ciliary structure and function in multiple tissues. Mechanistic investigation reveals that intraflagellar transport 88 (IFT88), a protein essential for ciliary assembly and maintenance, undergoes UFMylation at lysine 572. The UFMylation antagonizes IFT88 ubiquitination by Praja ring finger ubiquitin ligase 2 (PJA2), thereby preventing its proteasomal degradation. The lysine 572-to-arginine mutant of IFT88 exhibits increased stability and efficacy in rescuing ciliary defects induced by UFL1 depletion. Our findings identify a critical role for IFT88 UFMylation in ciliary homeostasis and offer novel insights into human ciliopathies.

Indexed as

CiliaProteinsUbiquitinationUbiquitin-Protein LigasesAnimalsHEK293 CellsHomeostasisHumansMiceMice, KnockoutProtein Processing, Post-TranslationalProteolysisProteinsUbiquitin-Protein Ligases

Identifiers

PMID41272290
PMCPMC13156313

What OpenQuestion holds

Textmetadata
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.