Two conserved glycine residues in mammalian and

Amino Acid Sequence Animals Dictyostelium / genetics Glycine / genetics Humans Mammals Mechanistic Target of Rapamycin Complex 2 / genetics Rapamycin-Insensitive Companion of mTOR Protein / genetics Structure-Activity Relationship
AKT Dictyostelium Mammalian target of rapamycin PKB Protein–protein interaction Rictor mTOR

Journal

Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457

Informations de publication

Date de publication:
14 11 2019
Historique:
received: 15 07 2019
accepted: 15 10 2019
pubmed: 28 10 2019
medline: 22 7 2020
entrez: 27 10 2019
Statut: epublish

Résumé

Mammalian, or mechanistic, target of rapamycin complex 2 (mTORC2) regulates a variety of vital cellular processes, and its aberrant functioning is often associated with various diseases. Rictor is a peculiar and distinguishing mTORC2 component playing a pivotal role in controlling its assembly and activity. Among extant organisms, Rictor is conserved from unicellular eukaryotes to metazoans. We replaced two distinct, but conserved, glycine residues in both the

Identifiants

DOI: 10.1242/jcs.236505 PMID: 31653780
pubmed: 31653780
pii: jcs.236505
doi: 10.1242/jcs.236505
pii:
doi:

Substances chimiques

Rapamycin-Insensitive Companion of mTOR Protein 0
Mechanistic Target of Rapamycin Complex 2 EC 2.7.11.1
Glycine TE7660XO1C

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2019. Published by The Company of Biologists Ltd.

Déclaration de conflit d'intérêts

Competing interestsThe authors declare no competing or financial interests.

Auteurs

Barbara Pergolizzi (B)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

Cristina Panuzzo (C)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

M Shahzad Ali (MS)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

Marco Lo Iacono (M)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

Chiara Levra Levron (C)

Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Centre, University of Torino, Via Nizza 52, 10126 Torino, Italy.

Luca Ponzone (L)

Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Centre, University of Torino, Via Nizza 52, 10126 Torino, Italy.

Marta Prelli (M)

Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Centre, University of Torino, Via Nizza 52, 10126 Torino, Italy.

Daniela Cilloni (D)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

Enzo Calautti (E)

Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Centre, University of Torino, Via Nizza 52, 10126 Torino, Italy.

Salvatore Bozzaro (S)

Department of Clinical and Biological Sciences, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy.

Enrico Bracco (E)

Department of Oncology, University of Torino, AOU S. Luigi, 10043 Orbassano (TO), Italy enrico.bracco@unito.it.
ORCID: 0000-0003-3170-2817

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Classifications MeSH

questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Eucaryotes › Animaux › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Eucaryotes › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Glycine › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Sérine-thréonine kinases TOR › Complexe-2 cible mécanistique de la rapamycine › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Sérine-thréonine kinases TOR › Complexe-2 cible mécanistique de la rapamycine › Compagnon de mTOR insensible à la rapamycine › Two conserved glycine residues in mammalian and
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Relation structure-activité › Two conserved glycine residues in mammalian and