Structural and biophysical analyses of the skeletal dihydropyridine receptor β subunit β_1a reveal critical roles of domain interactions for stability.

ABSTRACT: Excitation-contraction (EC) coupling in skeletal muscle requires a physical interaction between the voltage-gated calcium channel dihydropyridine receptor (DHPR) and the ryanodine receptor Ca²⁺ release channel. Although the exact molecular mechanism that initiates skeletal EC coupling is unresolved, it is clear that both the α₁ and β subunits of DHPR are essential for this process. Here, we employed a series of techniques, including size-exclusion chromatography-multi-angle light scattering, differential scanning fluorimetry, and isothermal calorimetry, to characterize various biophysical properties of the skeletal DHPR β subunit β_1a Removal of the intrinsically disordered N and C termini and the hook region of β_1a prevented oligomerization, allo

SUBMITTER: Norris NC 

PROVIDER: S-EPMC5437245 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature