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J Biol Chem, Vol. 274, Issue 16, 10677-10680, April 16, 1999
-Arrestin1-binding Protein
2-ADRENERGIC RECEPTOR
REGULATION
From the Howard Hughes Medical Institute and the Departments of
Medicine (Cardiology) and Biochemistry, Duke University Medical Center,
Durham, North Carolina 27710
Previous studies have demonstrated that
-arrestin1 serves to target G protein-coupled receptors for
internalization via clathrin-coated pits and that its endocytic
function is regulated by dephosphorylation at the plasma membrane.
Using the yeast two-hybrid system, we have identified a novel
-arrestin1-binding protein, NSF
(N-ethylmaleimide-sensitive fusion protein), an ATPase essential for many intracellular
transport reactions. We demonstrate that purified recombinant
-arrestin1 and NSF interact in vitro and that these
proteins can be coimmunoprecipitated from cells. -Arrestin1-NSF
complex formation exhibits a conformational dependence with
-arrestin1 preferentially interacting with the ATP bound form of
NSF. In contrast to the -arrestin1-clathrin interaction, however,
the phosphorylation state of -arrestin1 does not affect NSF binding.
Functionally, overexpression of NSF in HEK 293 cells significantly
enhances agonist-mediated 2-adrenergic receptor
(2-AR) internalization. Furthermore, when coexpressed with a -arrestin1 mutant (arr1S412D) that mimics a constitutively phosphorylated form of -arrestin1 and that acts as a dominant negative with regards to 2-AR internalization, NSF
rescues the arr1S412D-mediated inhibition of 2-AR
internalization. The demonstration of -arrestin1-NSF complex
formation and the functional consequences of NSF overexpression suggest
a hitherto unappreciated role for NSF in facilitating clathrin
coat-mediated G protein-coupled receptor internalization.
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