The N terminus of a schistosome beta subunit regulates inactivation and current density of a Cav2 channel.

ABSTRACT: The β subunit of high voltage-activated Ca(2+) (Ca(v)) channels targets the pore-forming α(1) subunit to the plasma membrane and tunes the biophysical phenotype of the Ca(v) channel complex. We used a combination of molecular biology and whole-cell patch clamp to investigate the functional role of a long N-terminal polyacidic motif (NPAM) in a Ca(v)β subunit of the human parasite Schistosoma mansoni (β(Sm)), a motif that does not occur in other known Ca(v)β subunits. When expressed in human embryonic kidney cells stably expressing Ca(v)2.3, β(Sm) accelerates Ca(2+)/calmodulin-independent inactivation of Ca(v)2.3. Deleting the first 44 amino acids of β(Sm), a region that includes NPAM, significantly slows the predominant time constant of inactivation (τ(fast)) under conditions that prevent

SUBMITTER: Salvador-Recatala V 

PROVIDER: S-EPMC2975211 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature