PMID- 10531415
OWN - NLM
STAT- MEDLINE
DCOM- 19991124
LR  - 20190607
IS  - 0026-895X (Print)
IS  - 0026-895X (Linking)
VI  - 56
IP  - 5
DP  - 1999 Nov
TI  - N-linked glycosylation is required for plasma membrane localization of D5, but
      not D1, dopamine receptors in transfected mammalian cells.
PG  - 1071-8
AB  - We have analyzed the role of N-linked glycosylation in functional cell surface
      expression of the D1 and D5 dopamine receptor subtypes. Treatment of transfected 
      HEK 293 cells with tunicamycin, an inhibitor of N-linked oligosaccharide
      addition, was found to prevent localization of D5 receptors in the plasma
      membrane. In contrast, tunicamycin treatment had no effect on the plasma membrane
      localization of the D1 receptor. Polymerase chain reaction mutagenesis was used
      to generate a panel of D5 receptors containing mutations in the three predicted
      sites of N-linked glycosylation. Expression of mutant receptors indicated that
      glycosylation of residue N7 was the major determinant of D5 receptor plasma
      membrane localization. Mutation of a comparable site in the D1 receptor at
      position N5 had no effect on the delivery of the D1 receptor to the cell surface.
      Tunicamycin treatment during receptor biosynthesis, but not N-glycosidase F
      digestion of mature receptors, abrogated binding of the D5 receptor antagonist
      [(3)H]SCH23390, suggesting that while oligosaccharide moieties play a key role in
      the cell surface expression of D5 receptors, they do not appear to contribute to 
      the receptor's ligand binding properties. Together, our data indicate a
      differential requirement for N-linked glycosylation in functional cell surface
      expression of D1 and D5 dopamine receptors.
FAU - Karpa, K D
AU  - Karpa KD
AD  - Department of Pharmacology, Penn State College of Medicine, Milton S. Hershey
      Medical Center, Hershey, Pennsylvania 17033, USA. kjd136@psu.edu
FAU - Lidow, M S
AU  - Lidow MS
FAU - Pickering, M T
AU  - Pickering MT
FAU - Levenson, R
AU  - Levenson R
FAU - Bergson, C
AU  - Bergson C
LA  - eng
GR  - MH56608/MH/NIMH NIH HHS/United States
GR  - P50-MH44866/MH/NIMH NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Pharmacol
JT  - Molecular pharmacology
JID - 0035623
RN  - 0 (DRD5 protein, human)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 0 (Receptors, Dopamine D1)
RN  - 11089-65-9 (Tunicamycin)
RN  - 137750-35-7 (Receptors, Dopamine D5)
SB  - IM
MH  - Cell Membrane/drug effects/*metabolism
MH  - Cells, Cultured
MH  - Glycosylation
MH  - Humans
MH  - Ligands
MH  - Mutation
MH  - Oligosaccharides/pharmacology
MH  - Receptors, Dopamine D1/genetics/*metabolism
MH  - Receptors, Dopamine D5
MH  - Transfection
MH  - Tunicamycin/pharmacology
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1124/mol.56.5.1071 [doi]
PST - ppublish
SO  - Mol Pharmacol. 1999 Nov;56(5):1071-8. doi: 10.1124/mol.56.5.1071.