Dianne M. Barry

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An in vivo experimental strategy, involving cardiac-specific expression of a mutant Kv 2.1 subunit that functions as a dominant negative, was exploited in studies focused on exploring the role of members of the Kv2 subfamily of pore-forming (a) subunits in the generation of functional voltage-gated K channels in the mammalian heart. A mutant Kv2.1 a subunit(More)
The protein Gle1 is required for export of mRNAs from the nucleus to the cytoplasm in both lower and higher eukaryotic cells. In human (h) cells, shuttling of hGle1 between the nucleus and cytoplasm is essential for bulk mRNA export. To date, no hGle1-interacting proteins have been reported and the mechanism by which hGle1 interacts with the nuclear pore(More)
The ion channel milieu present in a neuron in large part determines the inherent excitability of a given cell and is responsible for the translation of sensory transduction and synaptic input to axonal output. Intrinsic excitability is a dynamic process subject to multiple levels of regulation from channel gene expression to post-translational modifications(More)
Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four-amino acid segment, whereas hGle1B has a COOH-terminal 43-amino acid span. Only hGle1B, the(More)
A B S TRACT In the experiments here, the developmental expression of the functional Ca2+-independent, depolarization-activated K § channel currents, Ito and IK, and of the voltage-gated K + channel (Kv) 0t subunits, Kvl.2, Kvl.4, Kvl.5, Kv2.1, and Kv4.2 in rat ventricular myocytes were examined quantitatively. Using the whole-cell patch clamp recording(More)
Proteins transported into and out of the nucleus require amino acid motifs called NLSs and NESs, respectively. The amino acid sequences of these signals vary considerably. A superfamily of transport receptors has been identified and each member contains three transport-related domains. Transport receptors bind to the signal sequences, either directly or(More)
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