TY - GEN
T1 - Gating mechanisms of canonical transient receptor potential channel proteins
T2 - Role of phosphoinositols and diacylglycerol
AU - Albert, Anthony P.
N1 - Funding Information:
Work carried out in the laboratory of the author was funded by The Wellcome Trust and the British Heart Foundation. The author would like to thank Prof WA Large and Dr SN Saleh for many helpful discussions and for reading the manuscript.
PY - 2011
Y1 - 2011
N2 - Canonical transient receptor potential (TRPC) Ca 2+-permeable channels are members of the mammalian TRP super-family of cation channels, and have the closest homology to the founding members, TRP and TRPL, discovered in Drosophila photoreceptors. The TRPC subfamily is composed of 7 subunits (C1-C7, with TRPC2 a pseudogene in humans), which can all combine with one another to form homomeric and heteromeric structures. This review focuses on mechanisms involved in opening TRPC channels (i.e. gating mechanisms). It initially describes work on the involvement of phosphatidylinositol-4,5-bisphosphate (PIP 2) and diacylglycerol (DAG) in gating TRP and TRPL channels in Drosophila, and then discusses evidence that similar gating mechanisms are involved in opening mammalian TRPC channels. It concludes that there are two common activation pathways of mammalian TRPC channels. Non-TRPC1-containing channels are opened by interactions between DAG, the direct activating ligand, and PIP 2, which acts as a physiological antagonist at TRPC proteins. Competitive interactions between an excitatory effect of DAG and an inhibitory action of PIP 2 can also be modulated by IP 3 acting via an IP 3 receptor-independent mechanism. In contrast TRPC1-containing channels are gating by PIP 2, which requires PKC-dependent phosphorylation of TRPC1 proteins.
AB - Canonical transient receptor potential (TRPC) Ca 2+-permeable channels are members of the mammalian TRP super-family of cation channels, and have the closest homology to the founding members, TRP and TRPL, discovered in Drosophila photoreceptors. The TRPC subfamily is composed of 7 subunits (C1-C7, with TRPC2 a pseudogene in humans), which can all combine with one another to form homomeric and heteromeric structures. This review focuses on mechanisms involved in opening TRPC channels (i.e. gating mechanisms). It initially describes work on the involvement of phosphatidylinositol-4,5-bisphosphate (PIP 2) and diacylglycerol (DAG) in gating TRP and TRPL channels in Drosophila, and then discusses evidence that similar gating mechanisms are involved in opening mammalian TRPC channels. It concludes that there are two common activation pathways of mammalian TRPC channels. Non-TRPC1-containing channels are opened by interactions between DAG, the direct activating ligand, and PIP 2, which acts as a physiological antagonist at TRPC proteins. Competitive interactions between an excitatory effect of DAG and an inhibitory action of PIP 2 can also be modulated by IP 3 acting via an IP 3 receptor-independent mechanism. In contrast TRPC1-containing channels are gating by PIP 2, which requires PKC-dependent phosphorylation of TRPC1 proteins.
KW - Ca entry
KW - Ca -permeable cation channels
KW - Canonical transient receptor potential
KW - diacylglycerol
KW - inositol-1,4,5-trisphoshate
KW - phosphatidylinositol-4,5-bisphosphate
KW - phospholipase C
KW - protein kinase C
KW - receptor-operated channels
KW - store-operated channels
UR - http://www.scopus.com/inward/record.url?scp=79959804507&partnerID=8YFLogxK
U2 - 10.1007/978-94-007-0265-3_22
DO - 10.1007/978-94-007-0265-3_22
M3 - Conference contribution
C2 - 21290308
AN - SCOPUS:79959804507
SN - 9789400702646
T3 - Advances in Experimental Medicine and Biology
SP - 391
EP - 411
BT - Transient Receptor Potential Channels
A2 - Islam, Shahidul
A2 - Islam, Shahidul
ER -