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Differential Phosphorylation of Occludin and Tricellulin by CK2 and CK1.

Authors :
Dörfel, Max J.
Westphal, Julie K.
Huber, Otmar
Source :
Annals of the New York Academy of Sciences; May2009, Vol. 1165, p69-73, 5p, 2 Graphs
Publication Year :
2009

Abstract

In epithelial and endothelial cell layers tight junctions form selective apicolateral paracellular barriers separating luminal and extracellular spaces from the underlying tissues. Within the tight junctions the tetraspan transmembrane proteins occludin, claudins, and tricellulin form anastomosing strands of protein complexes, which interconnect opposing membranes of neighboring cells. Phosphorylation of tight junction components is critically involved in the regulation of tight junction assembly, maintenance, and function. This chapter compares occludin and tricellulin phosphorylation by the serine/threonine kinases CK2 and CK1. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00778923
Volume :
1165
Database :
Complementary Index
Journal :
Annals of the New York Academy of Sciences
Publication Type :
Academic Journal
Accession number :
40307230
Full Text :
https://doi.org/10.1111/j.1749-6632.2009.04043.x