Catalogue


Structural and Biophysical Studies of the Role of Stromal Interaction Molecules STIM1 and STIM2 in Initiating Store-operated Calcium Entry.
Zheng, Le.
imprint
2010.
description
108 leaves.
ISBN
9780494723609
format(s)
Microform, Thesis
Holdings
More Details
author
imprint
2010.
isbn
9780494723609
restrictions
Electronic version licensed for access by U. of T. users.
dissertation note
Thesis (M.Sc.)--University of Toronto, 2010.
general note
Source: Masters Abstracts International, Volume: 49-05, page: .
local note
ROBARTS MICROTEXT copy on microfiche.
abstract
Store-operated calcium entry (SOCE) is the major Ca 2+ entry pathway in most non-excitable cells maintaining prolonged elevation of cytosolic Ca2+ levels required for gene transcription. SOCE is activated by the loss of endoplasmic reticulum (ER) Ca2+ through stromal interaction molecules (STIM), ER-membrane associated Ca 2+ sensors. In humans, STIM1 and STIM2 share 65% sequence similarity but differentially regulate SOCE. Biophysical studies on the luminal Ca 2+-binding region suggests that STIM2 EF-SAM is more stable than STIM1. The NMR structure of Ca2+-loaded STIM2 EF-SAM determined in this work suggests a more stable SAM and a tighter EF-hand and SAM interaction in STIM2 may be account for its higher stability. Chimeric swapping of the EF-hand and SAM domains generates an unstable ES211. Introducing ES211 into cherryFP-STIM1 shows constitutive puncta which activate SOCE independent of ER depletion. The current work demonstrates that the instability of the EF-SAM plays an important role in regulating SOCE initiation.
catalogue key
7878733

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