J
Jeremy T. Blitzer
Researcher at Howard Hughes Medical Institute
Publications - 4
Citations - 1347
Jeremy T. Blitzer is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: PDZ domain & Receptor. The author has an hindex of 4, co-authored 4 publications receiving 1337 citations.
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Journal ArticleDOI
The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange.
Randy A. Hall,Richard T. Premont,Chung-Wai Chow,Jeremy T. Blitzer,Julie A. Pitcher,Audrey Claing,Robert H. Stoffel,Robert H. Stoffel,Larry S. Barak,Shirish Shenolikar,Edward J. Weinman,Edward J. Weinman,Edward J. Weinman,Sergio Grinstein,Robert J. Lefkowitz +14 more
TL;DR: It is reported here a direct agonist-promoted association of the β2-adrenergic receptor with the Na+/H+ exchanger regulatory factor (NHERF), a protein that regulates the activity of the Na-H- exchanger type 3 (NHE3).
Journal ArticleDOI
A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins.
Randy A. Hall,Lynda S. Ostedgaard,Richard T. Premont,Jeremy T. Blitzer,Nadeem Rahman,Michael J. Welsh,Robert J. Lefkowitz +6 more
TL;DR: The Na+/H+ exchanger regulatory factor (NHERF) binds to the tail of the beta2-adrenergic receptor and plays a role in adrenergic regulation of Na-H+ exchange and may be multifunctional adaptor proteins involved in many previously unsuspected aspects of intracellular signaling.
Journal ArticleDOI
Platelet-Derived Growth Factor Receptor Association with Na+/H+ Exchanger Regulatory Factor Potentiates Receptor Activity
Stuart Maudsley,A. Musa Zamah,Nadeem Rahman,Jeremy T. Blitzer,Louis M. Luttrell,Robert J. Lefkowitz,Randy A. Hall +6 more
TL;DR: NHERF can directly bind to the PDGFR and potentiatePDGFR activity, thus elucidating both a novel mechanism by which PDG FR activity can be regulated and a new cellular role for the PDZ domain-containing adapter protein NHERF.
Journal ArticleDOI
G Protein-coupled Receptor Kinase 6A Phosphorylates the Na+/H+ Exchanger Regulatory Factor via a PDZ Domain-mediated Interaction
Randy A. Hall,Robert F. Spurney,Richard T. Premont,Nadeem Rahman,Jeremy T. Blitzer,Julie A. Pitcher,Robert J. Lefkowitz +6 more
TL;DR: It is shown that the primary site of constitutive NHERF phosphorylated in human embryonic kidney 293 (HEK-293) cells is Ser289, and that the stoichiometry of phosphorylation is near 1 mol/mol, which indicates that the endogenous “NHERF kinase” activity in HEk-293 cell lysates is sensitive to treatments that alter the activity of GRK6A.