945
Views
6
CrossRef citations to date
0
Altmetric
Review

Roles of transient receptor potential channels in regulation of vascular and epithelial barriers

&
Article: e1331722 | Received 21 Feb 2017, Accepted 13 May 2017, Published online: 05 Jun 2017

Figures & data

Figure 1. Topology and domain structure of TRPC6. Each of the 4 TRPC6 monomers within a TRPC6 homotetramer contains 6 transmembrane domains with the pore region (LFW, pore motif) between domains 5 and 6. Structural domains for channel assembly and protein interaction sites are located on the cytoplasmic N and C termini. Figure adapted from ref. Citation2 with updates.

Figure 1. Topology and domain structure of TRPC6. Each of the 4 TRPC6 monomers within a TRPC6 homotetramer contains 6 transmembrane domains with the pore region (LFW, pore motif) between domains 5 and 6. Structural domains for channel assembly and protein interaction sites are located on the cytoplasmic N and C termini. Figure adapted from ref. Citation2 with updates.

Figure 2. Effector pathways from TRP channels that regulate barrier function. The ways that TRP channels influence barrier function include promoting intracellular tension by actin-myosin contraction mediated by calcium induced (1) activation of myosin light chain kinase (MLCK) through calmodulin (CaM), (2) RhoA activation of Rho kinase (ROCK) to inhibit inactivation of myosin phosphatase PP1c, (3) altering distribution of ZO-1 between tight junctions and cytoplasm, (4) endocytosis of occluding from tight junctions, and (5) direct interaction with catenins to influence their association with actin filaments.

Figure 2. Effector pathways from TRP channels that regulate barrier function. The ways that TRP channels influence barrier function include promoting intracellular tension by actin-myosin contraction mediated by calcium induced (1) activation of myosin light chain kinase (MLCK) through calmodulin (CaM), (2) RhoA activation of Rho kinase (ROCK) to inhibit inactivation of myosin phosphatase PP1c, (3) altering distribution of ZO-1 between tight junctions and cytoplasm, (4) endocytosis of occluding from tight junctions, and (5) direct interaction with catenins to influence their association with actin filaments.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.