PMID- 20332822
OWN - NLM
STAT- MEDLINE
DCOM- 20100707
LR  - 20211020
IS  - 1995-8218 (Electronic)
IS  - 1673-7067 (Print)
IS  - 1995-8218 (Linking)
VI  - 26
IP  - 2
DP  - 2010 Apr
TI  - Regulation of dopamine D3 receptors by protein-protein interactions.
PG  - 163-7
LID - 10.1007/s12264-010-1016-y [doi]
AB  - Galphai/o protein-coupled dopamine D3 receptors (D3Rs) are preferentially 
      expressed in the limbic system, including the nucleus accumbens. This situates 
      the receptor well in the regulation of limbic function and in the pathogenesis of 
      various neuropsychiatric and neurodegenerative disorders. The intracellular 
      domains of the receptor, mainly the large third intracellular loop and the 
      intracellular C-terminal tail, interact with multiple submembranous proteins. 
      These interactions are critical for the control of surface expression of the 
      receptor and the efficacy of receptor signaling. Recently, a synapse-enriched 
      protein kinase, Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), has been 
      found to interact with D3R in the above mentioned interaction model. CaMKII 
      directly binds to the N-terminal of the third loop of D3R. This binding is 
      Ca(2+)-dependent and is sustained by the autophosphorylation of the kinase. In 
      rat accumbal neurons, the increase in Ca(2+) level induces the recruitment of 
      CaMKII to D3R, and CaMKII phosphorylates the receptor at a specific serine site. 
      The CaMKII-induced phosphorylation could inhibit the receptor function and 
      further regulate the behavioral response to the psychostimulant cocaine. These 
      findings reveal a prototypic protein association model between a G 
      protein-coupled receptor and CaMKII. Through the dynamic protein-protein 
      interactions, the abundance, turnover cycle, and function of D3R can be regulated 
      by multiple signals and enzymatic proteins.
FAU - Guo, Ming-Lei
AU  - Guo ML
AD  - Department of Basic Medical Science, University of Missouri-Kansas City School of 
      Medicine, Saint Luke's Hospital, Kansas City, Missouri 64108, USA.
FAU - Liu, Xian-Yu
AU  - Liu XY
FAU - Mao, Li-Min
AU  - Mao LM
FAU - Wang, John Q
AU  - Wang JQ
LA  - eng
GR  - R01-DA010355/DA/NIDA NIH HHS/United States
GR  - R01 MH061469/MH/NIMH NIH HHS/United States
GR  - R01 MH061469-11/MH/NIMH NIH HHS/United States
GR  - R01-MH061469/MH/NIMH NIH HHS/United States
GR  - R01 DA010355-16/DA/NIDA NIH HHS/United States
GR  - R01 DA010355/DA/NIDA NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - Singapore
TA  - Neurosci Bull
JT  - Neuroscience bulletin
JID - 101256850
RN  - 0 (Receptors, Dopamine D3)
RN  - E0399OZS9N (Cyclic AMP)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
SB  - IM
MH  - Animals
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism
MH  - Cyclic AMP/metabolism
MH  - Humans
MH  - Limbic System/*metabolism
MH  - Models, Biological
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein Interaction Domains and Motifs/physiology
MH  - Receptors, Dopamine D3/*metabolism
MH  - Signal Transduction/*physiology
PMC - PMC2953790
MID - NIHMS236953
EDAT- 2010/03/25 06:00
MHDA- 2010/07/08 06:00
PMCR- 2011/04/01
CRDT- 2010/03/25 06:00
PHST- 2010/03/25 06:00 [entrez]
PHST- 2010/03/25 06:00 [pubmed]
PHST- 2010/07/08 06:00 [medline]
PHST- 2011/04/01 00:00 [pmc-release]
AID - 1016 [pii]
AID - 10.1007/s12264-010-1016-y [doi]
PST - ppublish
SO  - Neurosci Bull. 2010 Apr;26(2):163-7. doi: 10.1007/s12264-010-1016-y.