STIM1 protein studied by high resolution solid and solution state NMR
Sprache des Vortragstitels:
Englisch
Original Tagungtitel:
BISSL (Bilateral Impromptu Symposium (Stockholm-Linz) on NMR Spectroscopy
Sprache des Tagungstitel:
Englisch
Original Kurzfassung:
STIM1 is a calcium sensor protein in the endoplasmic reticulum which extends into
the cytosol and forms oligomers upon calcium store depletion. [1] The cytosolic part
of STIM1 consists of one long (CC1) and two short coiled coil domains involved in
homo-oligomerization and spatial elongation of the STIM1 protein leading to acti-
vation of the Orai/CRAC channel. [2] The Stormorken syndrome disease associated
with a single point mutation (R304W) within this region of STIM1 results in per-
manent activation of Orai channel. [3] Using high resolution solid and solution state
NMR we have found a helix elongation within the CC1 domain of the mutant close
to the mutation position with respect to the wild type STIM1. [4] These findings
corroborate the increased propensity of CC1 to form homomers destabilizing the
resting state of STIM1, which leads to the channel activation for the Stormorken
mutant.