Linking structure to function: Recent lessons from inositol 1,4,5-trisphosphate receptor mutagenesis.
Great insight has been gained into the structure and function of the inositol 1,4,5 trisphosphate receptor (InsP(3)R) by studies employing mutagenesis of the cDNA encoding the receptor. Notably, early studies using this approach defined the key constituents required for InsP(3) binding in the N-terminus and the membrane spanning regions in the C-terminal domain responsible for channel formation, targeting and function. In this article we evaluate recent studies which have used a similar approach to investigate key residues underlying the in vivo modulation by select regulatory factors. In addition, we review studies defining the structural requirements in the channel domain which comprise the conduction pathway and are suggested to be involved in the gating of the channel.
Department of Pharmacology and Physiology, University of Rochester, NY, United States. David_Yule@urmc.rochester.edu
David I
DI
Yule
Matthew J
MJ
Betzenhauser
Suresh K
SK
Joseph
D015220:Calcium Channels / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D017869:Cyclic GMP-Dependent Protein Kinases / Q000378:metabolism; D053496:Inositol 1,4,5-Trisphosphate Receptors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016296:Mutagenesis; D017434:Protein Structure, Tertiary
D015220:Calcium Channels; D053496:Inositol 1,4,5-Trisphosphate Receptors; D017868:Cyclic AMP-Dependent Protein Kinases; D017869:Cyclic GMP-Dependent Protein Kinases