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Identification and characterization ...

Wes, Paul D.

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Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling./
Author:	Wes, Paul D.
Description:	80 p.
Notes:	Source: Dissertation Abstracts International, Volume: 59-05, Section: B, page: 2062.
Contained By:	Dissertation Abstracts International59-05B.
Subject:	Biology, Neuroscience. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9833000
ISBN:	0591860538

Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling.
Wes, Paul D.

Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling. - 80 p.

Source: Dissertation Abstracts International, Volume: 59-05, Section: B, page: 2062.

Thesis (Ph.D.)--The Johns Hopkins University, 1998.

Ca

ISBN: 0591860538Subjects--Topical Terms:

1017680
Biology, Neuroscience.

Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling.
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020 $a 0591860538
035 $a (UnM)AAI9833000
035 $a AAI9833000
040 $a UnM $c UnM
100 1 $a Wes, Paul D. $3 1927862
245 1 0 $a Identification and characterization of store-operated channels and calmodulin-binding proteins in calcium signaling.
300 $a 80 p.
500 $a Source: Dissertation Abstracts International, Volume: 59-05, Section: B, page: 2062.
500 $a Adviser: Craig Montell.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 1998.
520 $a Ca $\ sp{2+} $ mediates signal transduction events in cells ranging from bacteria to neurons, yet the mechanisms by which Ca $\ sp{2+} $ integrates, modulates and relays signals remain poorly understood. The Drosophila visual system, which uses Ca $\ sp{2+} $ for sensory transduction and synaptic transmission, provides a unique opportunity for unraveling Ca $\ sp{2+} $ signaling, combining sensitive electrophysiological, genetic, biochemical, histological and molecular techniques.
520 $a A major enigma in the field of Ca $\ sp{2+} $ signaling involves the mechanism by which depletion of internal Ca $\ sp{2+} $ stores activates plasma membrane conductances mediated by putative store-operated channels (SOCs). By virtue of homology with the Drosophila protein, TRP, I identified and characterized the first vertebrate SOC subunits. Furthermore, to understand the function of Ca $\ sp{2+} $ in the Drosophila retina, I sought to identify new targets of the Ca $\ sp{2+} $- sensing regulatory protein, calmodulin (CaM). Various biochemical screens expanded the repertoire of known CaM-binding proteins in the Drosophila retina to include TRP; the PDZ domain-containing protein, INAD; synaptic proteins, such as Unc-13 and a Rab3-GEF; the cell adhesion molecule, Pollux; proteins with no homology to any factors in the database; and a variety of kinases and phosphatases, including the kinase-bearing unconventional myosin, NINAC. The two NINAC isoforms, p174 and p132, are spatially restricted to the rhabdomeres and cell bodies, respectively. NINAC p174 concentrates CaM in the phototransducing organelle, the rhabdomere, of the Drosophila photoreceptor, and is essential for adaptation and termination of the photoresponse. I mapped the rhabdomere localization signal of p174 to the C-terminal 96 residues. In addition, I found that NINAC bound to INAD via its C-terminal 21 residues. INAD also binds directly to many other mediators of phototransduction; thus, NINAC is a component of a supramolecular signaling complex through which it may contribute to adaptation and response termination.
520 $a One novel CaM-binding protein, RIC, belonged to the Ras family of monomeric GTPases. I identified two human homologs of RIC, RIN and RIT, thus defining a new subfamily of the Ras superfamily. I propose that the RIC family may mediate crosstalk between Ca $\ sp{2+} $ and Ras signaling.
590 $a School code: 0098.
650 4 $a Biology, Neuroscience. $3 1017680
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Animal Physiology. $3 1017835
650 4 $a Health Sciences, Ophthalmology. $3 1019445
690 $a 0317
690 $a 0307
690 $a 0379
690 $a 0433
690 $a 0381
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 59-05B.
790 1 0 $a Montell, Craig, $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 1998
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9833000