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Caldendrin, a brain-specific modulat...

Tippens, Alyssa.

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Caldendrin, a brain-specific modulator of calcium(v1.2) calcium(2+) channels.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Caldendrin, a brain-specific modulator of calcium(v1.2) calcium(2+) channels./
作者:	Tippens, Alyssa.
面頁冊數:	173 p.
附註:	Adviser: Amy Lee.
Contained By:	Dissertation Abstracts International68-09B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3279901
ISBN:	9780549217817

Caldendrin, a brain-specific modulator of calcium(v1.2) calcium(2+) channels.
Tippens, Alyssa.

Caldendrin, a brain-specific modulator of calcium(v1.2) calcium(2+) channels. - 173 p.

Adviser: Amy Lee.

Thesis (Ph.D.)--Emory University, 2007.

EF-hand Ca2+-binding proteins like calmodulin (CaM) and CaBP1 are potent modulators of voltage-gated Ca2+ channels. Caldendrin, a splice variant of CaBP1, interacts with Cav1.2 voltage-gated Ca2+ channels in a manner that distinguishes it from other Ca2+-binding proteins. Caldendrin binds to the C-terminal IQ-domain of Cav1.2 ((alpha11.2) and competitively displaces CaM and CaBP1 from this site. Moreover, mutations to the IQ-domain abolish physical interactions of caldendrin and Cav1.2. In contrast, caldendrin does not bind to the N-terminal domain of alpha11.2, a site that is critical for functional interactions with Cav1.2 and CaBP1. Caldendrin coimmunoprecipitates with Cav1.2 from the brain and colocalizes with Cav1.2 in somatodendritic puncta of cultured cortical neurons. These findings reveal heterogeneity within related Ca2+-binding proteins that may diversify the Ca2+ signaling of Cav 1.2 channels.

ISBN: 9780549217817Subjects--Topical Terms:

1017719
Biology, Molecular.

Caldendrin, a brain-specific modulator of calcium(v1.2) calcium(2+) channels.
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520 $a EF-hand Ca2+-binding proteins like calmodulin (CaM) and CaBP1 are potent modulators of voltage-gated Ca2+ channels. Caldendrin, a splice variant of CaBP1, interacts with Cav1.2 voltage-gated Ca2+ channels in a manner that distinguishes it from other Ca2+-binding proteins. Caldendrin binds to the C-terminal IQ-domain of Cav1.2 ((alpha11.2) and competitively displaces CaM and CaBP1 from this site. Moreover, mutations to the IQ-domain abolish physical interactions of caldendrin and Cav1.2. In contrast, caldendrin does not bind to the N-terminal domain of alpha11.2, a site that is critical for functional interactions with Cav1.2 and CaBP1. Caldendrin coimmunoprecipitates with Cav1.2 from the brain and colocalizes with Cav1.2 in somatodendritic puncta of cultured cortical neurons. These findings reveal heterogeneity within related Ca2+-binding proteins that may diversify the Ca2+ signaling of Cav 1.2 channels.
520 $a In the hippocampal formation, Cav1.2 voltage-gated Ca 2+ channels are involved in synaptic plasticity, the generation of spatial memories, and are thought to be localized to the cells bodies and proximal dendrites of hippocampal primary neurons, but electrophysiology studies suggest these channels are more broadly distributed. In situ hybridization indicates caldendrin is predominantly localized to the CA3 area, but biochemical evidence suggests a broader distribution in the hippocampal formation. Light level examination revealed (alpha11.2 immunoreactivity ((alpha 11.2-IR) was present in the pyramidal layer and dendritic fields of the CA1-CA3 areas and in the subfields of the dentate gyrus. By electron microscopy, (alpha11.2-IR was found in dendrites and spines, but also in axons and axon terminals in the dendritic subfields of the CA1 and CA3 areas. By light microscopy, caldendrin immunoreactivity (CD-IR) was detected in the pyramidal cell nuclei, soma, and dendritic fields of areas CA1-CA3 and in the granule cell soma and fibers in the dentate gyrus. At the electron microscopic level, CD-IR was primarily localized in glial elements, but also in various elements. These data provide the first detailed ultrastructural analysis of Cav1.2 and caldendrin localization in the hippocampal formation, suggests that Cav1.2 channels may play a role in integrating both pre- and post-synaptic inputs, and supports functionally diverse roles for caldendrin in Ca2+ signaling in glial and principal cells of the hippocampal formation.
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