当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > A serine point mutation in the adenosine A2AR C-terminal tail reduces receptor heteromerization and allosteric modulation of the dopamine D2R.

A serine point mutation in the adenosine A2AR C-terminal tail reduces receptor heteromerization and allosteric modulation of the dopamine D2R.

Abstract：

:Evidence exists that the adenosine receptor A(2A)R and the dopamine receptor D(2)R form constitutive heteromers in living cells. Mass spectrometry and pull-down data showed that an arginine-rich domain of the D(2)R third intracellular loop binds via electrostatic interactions to a specific motif of the A(2A)R C-terminal tail. It has been indicated that the phosphorylated serine 374 might represent an important residue in this motif. In the present study, it was found that a point mutation of serine 374 to alanine reduced the A(2A)R ability to interact with D(2)R. Also, this point mutation abolished the A(2A)R-mediated inhibition of both the D(2)R high affinity agonist binding and signaling. These results point to a key role of serine 374 in the A(2A)R-D(2)R interface. All together these results indicate that by targeting A(2A)R serine 374 it will be possible to allosterically modulate A(2A)R-D(2)R function, thus representing a new approach for therapeutically modulate D(2)R function.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Borroto-Escuela DO,Marcellino D,Narvaez M,Flajolet M,Heintz N,Agnati L,Ciruela F,Fuxe K

doi

10.1016/j.bbrc.2010.02.168

subject

Has Abstract

pub_date

2010-03-26 00:00:00

pages

222-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)00409-2

journal_volume

394

pub_type

杂志文章

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