PMID- 10393909
OWN - NLM
STAT- MEDLINE
DCOM- 19990826
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 14
DP  - 1999 Jul 6
TI  - Selective interaction of the C2 domains of phospholipase C-beta1 and -beta2 with 
      activated Galphaq subunits: an alternative function for C2-signaling modules.
PG  - 7843-6
AB  - Phospholipase C (PLC)-beta1 and PLC-beta2 are regulated by the Gq family of
      heterotrimeric G proteins and contain C2 domains. These domains are Ca2+-binding 
      modules that serve as membrane-attachment motifs in a number of signal
      transduction proteins. To determine the role that C2 domains play in PLC-beta1
      and PLC-beta2 function, we measured the binding of the isolated C2 domains to
      membrane bilayers. We found, unexpectedly, that these modules do not bind to
      membranes but they associate strongly and specifically to activated [guanosine
      5'-[gamma-thio]triphosphate (GTP[gammaS])-bound] Galphaq subunits. The C2 domain 
      of PLC-beta1 effectively suppressed the activation of the intact isozyme by
      Galphaq(GTP[gammaS]), indicating that the C2-Galphaq interaction may be
      physiologically relevant. C2 affinity for Galphaq(GTP[gammaS]) was reduced when
      Galphaq was deactivated to the GDP-bound state. Binding to activated Galphai1
      subunits or to Gbetagamma subunits was not detected. Also, Galphaq(GTP[gammaS])
      failed to associate with the C2 domain of PLC-delta, an isozyme that is not
      activated by Galphaq. These results indicate that the C2 domains of PLC-beta1 and
      PLC-beta2 provide a surface to which Galphaq subunits can dock, leading to
      activation of the native protein.
FAU - Wang, T
AU  - Wang T
AD  - Department of Physiology and Biophysics, State University of New York, Stony
      Brook, NY 11794-8661, USA.
FAU - Pentyala, S
AU  - Pentyala S
FAU - Elliott, J T
AU  - Elliott JT
FAU - Dowal, L
AU  - Dowal L
FAU - Gupta, E
AU  - Gupta E
FAU - Rebecchi, M J
AU  - Rebecchi MJ
FAU - Scarlata, S
AU  - Scarlata S
LA  - eng
GR  - R01 GM053132/GM/NIGMS NIH HHS/United States
GR  - GM43422/GM/NIGMS NIH HHS/United States
GR  - GM53132/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Isoenzymes)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteolipids)
RN  - 0 (Recombinant Proteins)
RN  - 0 (proteoliposomes)
RN  - 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 2.7.11.13 (Protein Kinase C-delta)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.11 (Phospholipase C beta)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - GTP-Binding Proteins/*chemistry/*metabolism
MH  - Guanosine 5'-O-(3-Thiotriphosphate)/metabolism
MH  - Isoenzymes/*chemistry/*metabolism
MH  - Kinetics
MH  - Macromolecular Substances
MH  - Peptide Fragments/*chemistry
MH  - Phospholipase C beta
MH  - Protein Kinase C/chemistry/metabolism
MH  - Protein Kinase C-delta
MH  - Proteolipids/metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Signal Transduction
MH  - Spodoptera
MH  - Transfection
MH  - Type C Phospholipases/*chemistry/*metabolism
PMC - PMC22149
EDAT- 1999/07/08 00:00
MHDA- 1999/07/08 00:01
CRDT- 1999/07/08 00:00
PHST- 1999/07/08 00:00 [pubmed]
PHST- 1999/07/08 00:01 [medline]
PHST- 1999/07/08 00:00 [entrez]
AID - 10.1073/pnas.96.14.7843 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7843-6. doi: 10.1073/pnas.96.14.7843.