Phospholipase C-gamma: diverse roles in receptor-mediated calcium signaling.
Ca2+ is a universal signal: the dynamic changes in its release and entry trigger a plethora of cellular responses. Central to this schema are members of the phospholipase C (PLC) superfamily, which relay information from the activated receptor to downstream signal cascades by production of second-messenger molecules. Recent studies reveal that, in addition to its enzymatic activity, PLC-gamma regulates Ca2+ entry via the formation of an intermolecular lipid-binding domain with canonical transient receptor potential 3 (TRPC3) ion channels. This complex, in turn, controls TRPC3 trafficking and cell-surface expression. Thus, TRPC3 ion channels are functionally linked to both lipase-dependent and -independent activities of PLC-gamma. Understanding the underlying molecular mechanisms that regulate this complex will probably clarify the processes of receptor-activated Ca2+ entry.
Patterson
Randen L
RL
Department of Biology, The Pennsylvania State University, Life Science Building, Shortlidge Road, University Park, PA 16801, USA.
van Rossum
Damian B
DB
Nikolaidis
Nikolas
N
Gill
Donald L
DL
Snyder
Solomon H
SH
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D020013:Calcium Signaling; D019143:Evolution, Molecular; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D051966:Phospholipase C gamma / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D050052:TRPC Cation Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D050052:TRPC Cation Channels; C104603:TRPC3 cation channel; D051966:Phospholipase C gamma