[HTML][HTML] Cloning and characterization of ATRAP, a novel protein that interacts with the angiotensin II type 1 receptor
The carboxyl-terminal cytoplasmic domain of the angiotensin II type 1 (AT 1) receptor has
recently been shown to interact with several classes of cytoplasmic proteins that regulate
different aspects of AT 1 receptor physiology. Employing yeast two-hybrid screening of a
mouse kidney cDNA library with the carboxyl-terminal cytoplasmic domain of the murine AT
1a receptor as a bait, we have isolated a novel protein with a predicted molecular mass of
18 kDa, which we have named ATRAP (for AT 1 receptor-associated protein). ATRAP …
recently been shown to interact with several classes of cytoplasmic proteins that regulate
different aspects of AT 1 receptor physiology. Employing yeast two-hybrid screening of a
mouse kidney cDNA library with the carboxyl-terminal cytoplasmic domain of the murine AT
1a receptor as a bait, we have isolated a novel protein with a predicted molecular mass of
18 kDa, which we have named ATRAP (for AT 1 receptor-associated protein). ATRAP …
