Abstract
The β-subunit of voltage-gated Ca2+ channels is essential for trafficking the channels to the plasma membrane and regulating their gating. It contains a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain, which interact intramolecularly. We investigated the structural underpinnings of this intramolecular coupling and found that in addition to a previously described SH3 domain β strand, two structural elements are crucial for maintaining a strong and yet potentially modifiable SH3-GK intramolecular coupling: an intrinsically weak SH3-GK interface and a direct connection of the SH3 and GK domains. Alterations of these elements uncouple the two functions of the β-subunit, degrading its ability to regulate gating while leaving its chaperone effect intact.
Original language | English (US) |
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Pages (from-to) | 1969-1975 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 12 |
DOIs | |
State | Published - Jun 18 2009 |
Keywords
- Auxiliary subunit
- Calcium channel
- Electrophysiology
- Membrane-associated guanylate kinase
- Regulation
- X-ray structure
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology