Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.
Amino Acid Sequence
/ genetics
Asparagine
/ genetics
Disease Progression
Drug Resistance, Neoplasm
/ genetics
Endoplasmic Reticulum
/ genetics
Glycosylation
Hexosyltransferases
/ genetics
Humans
Membrane Proteins
/ genetics
Neoplasms
/ drug therapy
Polysaccharides
/ genetics
Protein Processing, Post-Translational
/ genetics
N-glycosylation
endoplasmic reticulum
oligosaccharyltransfease
tumors
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
02 Dec 2019
02 Dec 2019
Historique:
received:
26
11
2019
revised:
28
11
2019
accepted:
28
11
2019
entrez:
8
12
2019
pubmed:
8
12
2019
medline:
18
4
2020
Statut:
epublish
Résumé
Oligosaccharyltransferase (OST) is a multi-span membrane protein complex that catalyzes the addition of glycans to selected Asn residues within nascent polypeptides in the lumen of the endoplasmic reticulum. This process, termed N-glycosylation, is a fundamental post-translational protein modification that is involved in the quality control, trafficking of proteins, signal transduction, and cell-to-cell communication. Given these crucial roles, N-glycosylation is essential for homeostasis at the systemic and cellular levels, and a deficiency in genes that encode for OST subunits often results in the development of complex genetic disorders. A growing body of evidence has also demonstrated that the expression of OST subunits is cell context-dependent and is frequently altered in malignant cells, thus contributing to tumor cell survival and proliferation. Importantly, a recently developed inhibitor of OST has revealed this enzyme as a potential target for the treatment of incurable drug-resistant tumors. This review summarizes our current knowledge regarding the functions of OST in the light of health and tumor progression, and discusses perspectives on the clinical relevance of inhibiting OST as a tumor treatment.
Identifiants
pubmed: 31810196
pii: ijms20236074
doi: 10.3390/ijms20236074
pmc: PMC6929149
pii:
doi:
Substances chimiques
Membrane Proteins
0
Polysaccharides
0
Asparagine
7006-34-0
Hexosyltransferases
EC 2.4.1.-
dolichyl-diphosphooligosaccharide - protein glycotransferase
EC 2.4.99.18
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : MEXT/JSPS Grants-in-Aid for Scientific Research
ID : 19K06546 to Y.H.
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