Structural organization of the tight junctions |
| |
Authors: | Luca Paris |
| |
Affiliation: | Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy |
| |
Abstract: | ![]() Tight junctions are the most apical organelle of the apical junctional complex and are primarily involved in the regulation of paracellular permeability and membrane polarity. Extensive research in the past two decades has identified not only the individual molecules of the tight junctions but also their mutual interactions, which are the focus of the present review article. While a complete map of the interactions among the tight junction molecules is probably far from being complete, the available evidence already allows outlining the general molecular architecture of the tight junctions. Here, with the aim of gaining deeper mechanistic understanding of tight junction assembly, regulation and function, we have subdivided the known molecular interactions into four major clusters that are centered on cell surface, polarity, cytoskeletal and signaling molecules. |
| |
Keywords: | aPKC, atypical protein kinase C GAP, GTPase-activating protein GST, glutathione-S-transferase JAM, junctional adhesion molecule LLGL1, lethal giant larvae-1 MAGI, membrane-associated guanylate kinase with inverted orientation MAGUK, membrane-associated guanylate kinases MDCK, Madin-Derby canine kidney MUPP1, multi-PDZ domain protein-1 PI3K, phosphatidyl-inositol 3-kinase PICK-1, protein interacting with protein C kinase-1 TGF-β, transforming growth factor-β TJ, tight junctions ZO, zonula occludens ZONAB, ZO-1-associated nucleic acid binding |
本文献已被 ScienceDirect 等数据库收录! |
|