TRP Channels

TRP Channels

New Book on TRP Channels

Read it online. Get your copy from Amazon. Get your copy from Springer.

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 13

AbstractsPosted by Md. Shahidul Islam Wed, February 16, 2011 16:53:25

The TRPML3 Channel: From Gene to Function

Konrad Noben-Trauth

Abstract TRPML3 is a transient receptor potential (TRP) channel that is encoded by the mucolipin 3 gene (MCOLN3), a member of the small mucolipin gene family. Mcoln3 shows a broad expression pattern in embryonic and adult tissues that includes differentiated cells of skin and inner ear. Dominant mutant alleles of murine Mcoln3 cause embryonic lethality, pigmentation defects and deafness. The TRPML3 protein features a six-transmembrane topology and functions as a Ca2+ permeable inward rectifying cation channel that is open at sub-physiological pH and closes as the extracytosolic pH becomes more acidic. TRPML3 localizes to the plasmamembrane and to early- and late-endosomes as well as lysosomes. Recent advances suggest that TRPML3 may regulate the acidification of early endosomes, hence playing a critical role in the endocytic pathway.

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