Alterations of Golgi Structural Proteins and Glycosylation Defects in Cancer.
COG complex
GM130
GRASP55
Golgi fragmentation
Golgi matrix
cancer
glycosylation
Journal
Frontiers in cell and developmental biology
ISSN: 2296-634X
Titre abrégé: Front Cell Dev Biol
Pays: Switzerland
ID NLM: 101630250
Informations de publication
Date de publication:
2021
2021
Historique:
received:
07
02
2021
accepted:
19
04
2021
entrez:
31
5
2021
pubmed:
1
6
2021
medline:
1
6
2021
Statut:
epublish
Résumé
As the central hub in the secretory and endocytic pathways, the Golgi apparatus continually receives the flow of cargos and serves as a major processing station in the cell. Due to its dynamic nature, a sophisticated and constantly remodeling mechanism needs to be set up to maintain the Golgi architecture and function in the non-stop trafficking of proteins and lipids. Abundant evidence has been accumulated that a well-organized Golgi structure is required for its proper functions, especially protein glycosylation. Remarkably, altered glycosylation has been a hallmark of most cancer cells. To understand the causes of Golgi defects in cancer, efforts have been made to characterize Golgi structural proteins under physiological and pathological conditions. This review summarizes the current knowledge of crucial Golgi structural proteins and their connections with tumor progression. We foresee that understanding the Golgi structural and functional defects may help solve the puzzle of whether glycosylation defect is a cause or effect of oncogenesis.
Identifiants
pubmed: 34055798
doi: 10.3389/fcell.2021.665289
pmc: PMC8149618
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
665289Informations de copyright
Copyright © 2021 Zhang.
Déclaration de conflit d'intérêts
The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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