TY - JOUR
T1 - Phospholipase C-γ
T2 - Diverse roles in receptor-mediated calcium signaling
AU - Patterson, Randen L.
AU - Van Rossum, Damian B.
AU - Nikolaidis, Nikolas
AU - Gill, Donald L.
AU - Snyder, Solomon H.
N1 - Funding Information:
This research was supported by US Public Health Service Grants MH-18501 and DA-000266, Research Scientist Award DA-00074 (S.H.S.) and National Institutes of Health Grant HL55426 (D.L.G.). We acknowledge Dimitra Chalkia and Kyung De Ko for their role in developing the GDDA and thank M. Mathers III and A. Dre for useful discussion.
PY - 2005/12
Y1 - 2005/12
N2 - 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-γ 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-γ. Understanding the underlying molecular mechanisms that regulate this complex will probably clarify the processes of receptor-activated Ca 2+ entry.
AB - 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-γ 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-γ. Understanding the underlying molecular mechanisms that regulate this complex will probably clarify the processes of receptor-activated Ca 2+ entry.
UR - http://www.scopus.com/inward/record.url?scp=27944458450&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=27944458450&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2005.10.005
DO - 10.1016/j.tibs.2005.10.005
M3 - Review article
C2 - 16260143
AN - SCOPUS:27944458450
SN - 0968-0004
VL - 30
SP - 688
EP - 697
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 12
ER -