Tight junction proteins occludin and ZO-1 as regulators of epithelial proliferation and survival.
actin
barrier
claudin
intestine
permeability
Journal
Annals of the New York Academy of Sciences
ISSN: 1749-6632
Titre abrégé: Ann N Y Acad Sci
Pays: United States
ID NLM: 7506858
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
pubmed:
18
5
2022
medline:
1
9
2022
entrez:
17
5
2022
Statut:
ppublish
Résumé
Epithelial cells are the first line of mucosal defense. In the intestine, a single layer of epithelial cells must establish a selectively permeable barrier that supports nutrient absorption and waste secretion while preventing the leakage of potentially harmful luminal materials. Key to this is the tight junction, which seals the paracellular space and prevents unrestricted leakage. The tight junction is a protein complex established by interactions between members of the claudin, zonula occludens, and tight junction-associated MARVEL protein (TAMP) families. Claudins form the characteristic tight junction strands seen by freeze-fracture microscopy and create paracellular channels, but the functions of ZO-1 and occludin, founding members of the zonula occludens and TAMP families, respectively, are less well defined. Recent studies have revealed that these proteins have essential noncanonical (nonbarrier) functions that allow them to regulate epithelial apoptosis and proliferation, facilitate viral entry, and organize specialized epithelial structures. Surprisingly, neither is required for intestinal barrier function or overall health in the absence of exogenous stressors. Here, we provide a brief overview of ZO-1 and occludin canonical (barrier-related) functions, and a more detailed examination of their noncanonical functions.
Identifiants
pubmed: 35580994
doi: 10.1111/nyas.14798
pmc: PMC9427709
mid: NIHMS1802682
doi:
Substances chimiques
Claudins
0
Occludin
0
Tight Junction Proteins
0
Zonula Occludens-1 Protein
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
21-33Subventions
Organisme : NIDDK NIH HHS
ID : P30 DK034854
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK061931
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK068271
Pays : United States
Organisme : NIDDK NIH HHS
ID : T32 DK007074
Pays : United States
Informations de copyright
© 2022 New York Academy of Sciences.
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