FKBP10 Regulates Protein Translation to Sustain Lung Cancer Growth.

Animals Carcinogenesis / pathology Cell Line, Tumor Cell Proliferation Down-Regulation Lung Neoplasms / metabolism Mice, Inbred NOD Mice, SCID Neoplastic Stem Cells / metabolism Peptidylprolyl Isomerase / metabolism Protein Biosynthesis Proto-Oncogene Proteins p21(ras) / metabolism Ribosomes / metabolism Tacrolimus Binding Proteins / metabolism

Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
17 03 2020
Historique:
received: 10 06 2017
revised: 29 10 2019
accepted: 20 02 2020
entrez: 19 3 2020
pubmed: 19 3 2020
medline: 24 3 2021
Statut: ppublish

Résumé

Cancer therapy is limited, in part, by lack of specificity. Thus, identifying molecules that are selectively expressed by, and relevant for, cancer cells is of paramount medical importance. Here, we show that peptidyl-prolyl-cis-trans-isomerase (PPIase) FK506-binding protein 10 (FKBP10)-positive cells are present in cancer lesions but absent in the healthy parenchyma of human lung. FKBP10 expression negatively correlates with survival of lung cancer patients, and its downregulation causes a dramatic diminution of lung tumor burden in mice. Mechanistically, our results from gain- and loss-of-function assays show that FKBP10 boosts cancer growth and stemness via its PPIase activity. Also, FKBP10 interacts with ribosomes, and its downregulation leads to reduction of translation elongation at the beginning of open reading frames (ORFs), particularly upon insertion of proline residues. Thus, our data unveil FKBP10 as a cancer-selective molecule with a key role in translational reprogramming, stem-like traits, and growth of lung cancer.

Identifiants

DOI: 10.1016/j.celrep.2020.02.082 PMID: 32187554
pubmed: 32187554
pii: S2211-1247(20)30256-4
doi: 10.1016/j.celrep.2020.02.082
pii:
doi:

Substances chimiques

Hras protein, mouse EC 3.6.5.2
Proto-Oncogene Proteins p21(ras) EC 3.6.5.2
Tacrolimus Binding Proteins EC 5.2.1.-
FKBP10 protein, human EC 5.2.1.8
Peptidylprolyl Isomerase EC 5.2.1.8

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3851-3863.e6

Informations de copyright

Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Interests The authors declare no competing interests.

Auteurs

Giorgio Ramadori (G)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland. Electronic address: giorgio.ramadori@unige.ch.

Rafael M Ioris (RM)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Zoltan Villanyi (Z)

Department of Microbiology and Molecular Medicine, Institute of Genetics and Genomics, Facutly of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Raquel Firnkes (R)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Olesya O Panasenko (OO)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Department of Infectious Diseases, Hôpitaux Universitaires de Genève, Genève, Switzerland.

George Allen (G)

Department of Microbiology and Molecular Medicine, Institute of Genetics and Genomics, Facutly of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Georgia Konstantinidou (G)

Institute of Pharmacology, University of Bern, 3010 Bern, Switzerland.

Ebru Aras (E)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Xavier Brenachot (X)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Tommasina Biscotti (T)

Section of Pathological Anatomy, Department of Biomedical Sciences and Public Health, Università Politecnica delle Marche, 60020 Ancona, Italy.

Anne Charollais (A)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland.

Michele Luchetti (M)

Clinica Medica, Dipartimento di Scienze Cliniche e Molecolari, Università Politecnica delle Marche, 60020 Ancona, Italy.

Fedor Bezrukov (F)

School of Physics and Astronomy, University of Manchester, Oxford Road, Manchester M13 9PL, UK.

Alfredo Santinelli (A)

Section of Pathological Anatomy, Department of Biomedical Sciences and Public Health, Università Politecnica delle Marche, 60020 Ancona, Italy.

Muntaha Samad (M)

Department of Computer Science, University of California, Irvine, Irvine, CA 92697, USA; Institute for Genomics and Bioinformatics, University of California, Irvine, Irvine, CA 92697, USA.

Pierre Baldi (P)

Department of Computer Science, University of California, Irvine, Irvine, CA 92697, USA; Institute for Genomics and Bioinformatics, University of California, Irvine, Irvine, CA 92697, USA.

Martine A Collart (MA)

Department of Microbiology and Molecular Medicine, Institute of Genetics and Genomics, Facutly of Medicine, University of Geneva, 1211 Geneva, Switzerland. Electronic address: martine.collart@unige.ch.

Roberto Coppari (R)

Department of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland; Diabetes Center of the Faculty of Medicine, University of Geneva, 1211 Geneva, Switzerland. Electronic address: roberto.coppari@unige.ch.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Processus néoplasiques › Carcinogenèse › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Cellules › Cellules cultivées › Cellules cancéreuses en culture › Lignée cellulaire tumorale › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Phénomènes physiologiques › Croissance et développement › Croissance › Processus de croissance cellulaire › Prolifération cellulaire › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Régulation négative › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Maladies de l'appareil respiratoire › Tumeurs de l'appareil respiratoire › Tumeurs du poumon › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Lignées consanguines de souris › Souris de lignée NOD › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souches mutantes de souris › Souris SCID › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Cellules › Cellules souches › Cellules souches tumorales › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Cis-trans-isomerases › Peptidylpropyl isomerase › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Phénomènes génétiques › Expression des gènes › Biosynthèse des protéines › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines tumorales › Protéines oncogènes › Protéines proto-oncogènes › Protéines proto-oncogènes p21(ras) › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Ribosomes › FKBP10 Regulates Protein Translation to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Récepteurs des médicaments › Immunophilines › Protéines de liaison au tacrolimus › FKBP10 Regulates Protein Translation to...