12.02.2013 Views

New Modes of GPCR Signalling

New Modes of GPCR Signalling

New Modes of GPCR Signalling

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

ABSTRACT<br />

Structural Feature and Function <strong>of</strong> hβ-subunits <strong>of</strong> BK Channel<br />

Jiuping Ding<br />

Key Laboratory <strong>of</strong> Molecular Biophysics Ministry <strong>of</strong> Education, College <strong>of</strong> Life<br />

Science and Technology, Huazhong University <strong>of</strong> Science and Technology, Wuhan,<br />

Hubei, 430074, China<br />

The functional diversity <strong>of</strong> large conductance Ca 2+ - and voltage-dependent K + (BK)<br />

channels arises mainly from co-assembly <strong>of</strong> the pore-forming mSlo α subunits with four<br />

tissue enriched auxiliary β subunits. The structural basis <strong>of</strong> the interaction between α<br />

subunits with β subunits is not well understood.<br />

Using immun<strong>of</strong>luorescence and patch clamp techniques, we demonstrated that 1)<br />

four-turn α-helical segment prevents surface expression <strong>of</strong> the auxiliary hβ2 subunit <strong>of</strong><br />

BK-type channel; 2) lysine-rich extracellular rings formed by hβ2 subunits confer the<br />

outward rectification <strong>of</strong> BK channels; 3) structural basis for toxin resistance <strong>of</strong><br />

β4-associated calcium-activated potassium (BK) channels. Those findings provide a<br />

better understanding <strong>of</strong> the structure and the diverse interactions between α and β<br />

subunits and will improve the design <strong>of</strong> channel inhibitors.

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!