Molecular Pathways of Interferon-Stimulated Gene 15: Implications in Cancer.
Cytokines
/ chemistry
Gene Expression Regulation, Neoplastic
Humans
Immunity, Innate
Interferon-alpha
/ genetics
Interferon-beta
/ genetics
Intracellular Signaling Peptides and Proteins
/ genetics
Models, Molecular
Neoplasms
/ genetics
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Processing, Post-Translational
Signal Transduction
Ubiquitin Thiolesterase
/ genetics
Ubiquitin-Conjugating Enzymes
/ genetics
Ubiquitination
Ubiquitins
/ chemistry
Free ISG15
ISGylation system
cancer
conjugated ISG15
molecular pathways
proteins
Journal
Current protein & peptide science
ISSN: 1875-5550
Titre abrégé: Curr Protein Pept Sci
Pays: United Arab Emirates
ID NLM: 100960529
Informations de publication
Date de publication:
2021
2021
Historique:
received:
28
07
2020
revised:
18
10
2020
accepted:
02
11
2020
pubmed:
10
12
2020
medline:
29
5
2021
entrez:
9
12
2020
Statut:
ppublish
Résumé
Human interferon-stimulated gene 15 (ISG15) is a 15-kDa ubiquitin-like protein that can be detected as either free ISG15 or covalently associated with its target proteins through a process termed ISGylation. Interestingly, extracellular free ISG15 has been proposed as a cytokinelike protein, whereas ISGylation is a posttranslational modification. ISG15 is a small protein with implications in some biological processes and pathologies that include cancer. This review highlights the findings of both free ISG15 and protein ISGylation involved in several molecular pathways, emerging as central elements in some cancer types.
Identifiants
pubmed: 33292152
pii: CPPS-EPUB-112186
doi: 10.2174/1389203721999201208200747
doi:
Substances chimiques
Cytokines
0
HERC5 protein, human
0
Interferon-alpha
0
Intracellular Signaling Peptides and Proteins
0
Ubiquitins
0
ISG15 protein, human
60267-61-0
Interferon-beta
77238-31-4
UBE2L6 protein, human
EC 2.3.2.23
Ubiquitin-Conjugating Enzymes
EC 2.3.2.23
USP18 protein, human
EC 3.4.19.12
Ubiquitin Thiolesterase
EC 3.4.19.12
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
19-28Informations de copyright
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.