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January 24, 2010 | History

Direct physical and functional interaction of esophageal smooth muscle Kv1.2 with a distinct Syntaxin1A conformation 1 edition

Direct physical and functional interaction of esophageal smooth muscle ...
Leila Neshatian

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Direct physical and functional interaction of esophageal smooth muscle Kv1.2 with a distinct Syntaxin1A conformation.

Published 2005 .
Written in English.

About the Book

SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) regulate activity and cell surface distribution of ion channels through direct physical interactions with the channels. I examined the structure-functional interactions between KV1.2, an important delayed rectifier K + channel in esophageal smooth muscle (ESM), and different Syntaxin1A (Syn1A) proteins. Wild type (WT) Syn1A, unlike the open form, potently inhibited KV1.2 currents and channel kinetics in the KV1.2-expressing HEK293 cells. WT and open form Syn1A and the H3-domain of Syn1A but not its HABC-domain bound ESM and tsA cell extracts' KV1.2. The inhibition of KV1.2 by WT Syn1A is not due to a defect in channel surfacing. In fact, WT Syn1A increased KV1.2 channel surfacing. Therefore, the H3-KV1.2 linkage within a closed conformation of Syn1A conveys the functional inhibition of the ESM KV1.2. This thesis provides the first evidence that the structure-function relationships are different between secretory cells and non-secretory cells such as ESM.

Edition Notes

Source: Masters Abstracts International, Volume: 44-02, page: 0736.

Thesis (M.Sc.)--University of Toronto, 2005.

Electronic version licensed for access by U. of T. users.

GERSTEIN MICROTEXT copy on microfiche (2 microfiches).

The Physical Object

Pagination
117 leaves.
Number of pages
117

ID Numbers

Open Library
OL19217809M
ISBN 10
0494074973

History Created December 11, 2009 · 2 revisions Download catalog record: RDF / JSON

January 24, 2010 Edited by WorkBot add more information to works
December 11, 2009 Created by WorkBot add works page