TRP Channels

TRP Channels

New Book on TRP Channels

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Transient Receptor Potential Channels offers a unique blend of thoughtfully selected topics ranging from the structural biology of this fascinating group of ion channels to their emerging roles in human diseases. This single book covers TRP channels of yeasts, flies, fishes frogs and humans. And from the biophysics of primary thermo-sensory events in cells to the thermosensation at whole organism level, from physiology of pain to the development of pain-killers, from psychiatric illnesses to cancers, from skin cells to sperms, from taste buds to testes, from established facts to heated debates, this book contains something for every TRP enthusiasts, beginner and expert alike. It includes crucial background information, critical analysis of cutting edge research, and ideas and thoughts for numerous testable hypotheses. It also shows directions for future research in this highly dynamic field. It is a book readers will be just as eager to give to others as keep for themselves. Transient Receptor Potential Channels (Advances in Experimental Medicine and Biology) [Hard cover]. Md. Shahidul Islam (Editor). Publisher: Springer. 52 chapters, 125 authors, about 1115 pages

Chapter 22

AbstractsPosted by Md. Shahidul Islam Mon, February 07, 2011 18:58:55

Gating Mechanisms of Canonical Transient Receptor Potential Channel Proteins: Role of Phosphoinositols and Diacylglycerol

Anthony P. Albert

Canonical transient receptor potential (TRPC) Ca2+-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 (PIP2) 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 PIP2, which acts as a physiological antagonist at TRPC proteins. Competitive interactions between an excitatory effect of DAG and an inhibitory action of PIP2 can also be modulated by IP3 acting via an IP3 receptor-independent mechanism. In contrast TRPC1-containing channels are gating by PIP2, which requires PKC-dependent phosphorylation of TRPC1 proteins.

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