Sensing with Ion Channels by Ching Kung, Xin-Liang Zhou, Zhen-Wei Su, W. John Haynes
By Ching Kung, Xin-Liang Zhou, Zhen-Wei Su, W. John Haynes (auth.), Professor Boris Martinac (eds.)
All dwelling cells may be able to discover and translate environmental stimuli into biologically significant signs. Sensations of contact, listening to, sight, style, scent or ache are necessary to the survival of all dwelling organisms. the significance of sensory enter for the lifestyles of existence hence justifies the trouble made to appreciate its molecular origins. Sensing with Ion Channels makes a speciality of ion channels as key molecules permitting organic platforms to feel and procedure the actual and chemical stimuli that act upon cells of their dwelling atmosphere. Its goal is to function a connection with ion channel experts and as a resource of recent details to non experts who are looking to know about the structural and practical range of ion channels and their position in sensory physiology.
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Sample text
The most obvious channel activities observed in such native bacterial membranes are mechanosensitive channels. In the original report, only a single activity was reported (Martinac et al. 1987); however, we now know that there are at least four mechanosensitive channel activities in E. coli: MscL (mechanosensitive channel of large conductance), MscS (smaller), MscK (K+-regulated) and MscM (mini). MscL truly is of large conductance, being over 3 nanosiemens (nS), which is approximately 100-fold greater than that of most eukaryotic channels.
Once these molecular targets are found, their sequence homologs can be recognized and used in further research. Commonly, mammalian homologs are heterologously expressed in oocytes or cultured cells and examined biophysically or biochemically. Knock-out mice are also generated to examine possible phenotypes. These studies are generically referred to as “reverse genetics”, and constitute the bulk of current research in this field, as reviewed in the chapters by Hamill and Moroto (Chap. 7), Liedtke (Chap.
Site-directed mutagenesis confirmed that channel activity could be modified by structural changes to the protein (Blount et al. 1996b, 1997), and a random mutagenesis study implicated the cytoplasmic half of the first transmembrane domain (TMD1) as a mutagenic ‘hot spot’, implying its importance in mechanosensitive channel function (Ou et al. 1998; Maurer and Dougherty 2003). Many of the predictions were confirmed and others resolved when a crystal structure of a homologue from Mycobacterium tuberculosis (Tb-MscL) was obtained (Chang et al.