Evidence map›Paper›PMID 33064845›Full record

ArticleFEBS letters2021

Ciliary localization of folliculin mediated via a kinesin-2-binding motif is required for its functions in mTOR regulation and tumor suppression.

Yunlong Zhang, Ying Liu, Yu Dai, Yazhe Ren, Guangsen Bao, Bo Ai, Yu Jiang

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2021. 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
0.7field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

7 authors at 2 institutions in 2 countries.

Yunlong ZhangDepartment of Bioengineering, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, Shanghai, China.
Ying LiuDepartment of Pharmacology and Chemical Biology, University of Pittsburgh, PA, USA.
Yu DaiDepartment of Pharmacology and Chemical Biology, University of Pittsburgh, PA, USA.
Yazhe RenDepartment of Bioengineering, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, Shanghai, China.
Guangsen BaoDepartment of Bioengineering, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, Shanghai, China.
Bo AiDepartment of Pharmacology and Chemical Biology, University of Pittsburgh, PA, USA.
Yu JiangDepartment of Pharmacology and Chemical Biology, University of Pittsburgh, PA, USA.ORCID 0000-0003-4746-1528
University of Pittsburgh · USDonghua University · CN

Funding

Investigating the Impact and Patterns of Homologous Recombination and Adaptive Evolution on Bacterial GenomesR01GM132137 · NIGMS · UNIVERSITY OF NORTH CAROLINA GREENSBORO · PI BOBAY, LOUIS-MARIE · 2020 to 2024
$1.5M
Mechanisms of Signaling Protein Retention in the Primary CiliumR01GM132127 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JIANG, YU · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM132127NIGMS NIH HHS R01 GM132137
6 · The paper itself

Abstract

Folliculin (FLCN) is a tumor suppressor protein involved in many cellular processes, including cell signaling, apoptosis, and autophagy. In ciliated cells, FLCN localizes to primary cilia and controls mTORC1 signaling in response to flow stress. Here, we show that the ciliary localization of FLCN requires its interaction with kinesin-2, the motor protein for anterograde intraflagellar transport. FLCN binds to kinesin-2 through a loop region in the middle of the protein. Single point mutations within this region of FLCN disrupt its kinesin-2 binding and ciliary entry. The mutants lose the ability to suppress the abnormal mTORC1/2 signaling activities and anchorage-independent growth of FLCN-deficient tumor cells. These observations suggest that ciliary localization of FLCN is essential for its function as a tumor suppressor.

Indexed as

Genes, Tumor SuppressorAmino Acid SequenceCiliaHEK293 CellsHumansKinesinsPoint MutationProtein BindingProto-Oncogene ProteinsTOR Serine-Threonine KinasesTumor Suppressor ProteinsFLCN protein, humanKIF2A protein, humanKinesinsMTOR protein, humanProto-Oncogene ProteinsTOR Serine-Threonine KinasesTumor Suppressor ProteinsciliumFLCNkinesin-2mTORC1mTORC2

Identifiers

PMID33064845
PMCPMC7980781
OpenAlexW3093202716

What OpenQuestion holds

Textmetadata
LicenceTDM
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.