Jamaica Bay: An Urban Marshland in Transition

This article will briefly examine the environmental problems that affect the lives of the hundreds of thousands of people who live adjacent to Jamaica Bay, and the extraordinary opportunities for recreation and enjoyment for which the Bay, freed of sewage, air pollution and aircraft noise, could be employed

67/10/25 Brief of Attorney General of the State of New York as Amicus Curiae in Support of Appellees

New York Attorney General Amicus Curiae brief argues that police should be able to stop and question suspects whom they reasonably believe have or are planning to commit a felony

67/10/25 Brief of Attorney General of the State of New York as Amicus Curiae in Support of Appellees

New York Attorney General Amicus Curiae brief argues that police should be able to stop and question suspects whom they reasonably believe have or are planning to commit a felony

Platelet-Derived Growth Factor Receptor Association with Na(+)/H(+) Exchanger Regulatory Factor Potentiates Receptor Activity

Platelet-derived growth factor (PDGF) is a potent mitogen for many cell types. The PDGF receptor (PDGFR) is a receptor tyrosine kinase that mediates the mitogenic effects of PDGF by binding to and/or phosphorylating a variety of intracellular signaling proteins upon PDGF-induced receptor dimerization. We show here that the Na(+)/H(+) exchanger regulatory factor (NHERF; also known as EBP50), a protein not previously known to interact with the PDGFR, binds to the PDGFR carboxyl terminus (PDGFR-CT) with high affinity via a PDZ (PSD-95/Dlg/Z0-1 homology) domain-mediated interaction and potentiates PDGFR autophosphorylation and extracellular signal-regulated kinase (ERK) activation in cells. A point-mutated version of the PDGFR, with the terminal leucine changed to alanine (L1106A), cannot bind NHERF in vitro and is markedly impaired relative to the wild-type receptor with regard to PDGF-induced autophosphorylation and activation of ERK in cells. NHERF potentiation of PDGFR signaling depends on the capacity of NHERF to oligomerize. NHERF oligomerizes in vitro when bound with PDGFR-CT, and a truncated version of the first NHERF PDZ domain that can bind PDGFR-CT but which does not oligomerize reduces PDGFR tyrosine kinase activity when transiently overexpressed in cells. PDGFR activity in cells can also be regulated in a NHERF-dependent fashion by stimulation of the β(2)-adrenergic receptor, a known cellular binding partner for NHERF. These findings reveal that NHERF can directly bind to the PDGFR and potentiate PDGFR activity, thus elucidating both a novel mechanism by which PDGFR activity can be regulated and a new cellular role for the PDZ domain-containing adapter protein NHERF

Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation

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