Abstract:
:Despite the fact that the phosphorylation-mediated regulation of L-type Ca channels is viewed as a model of ion channel regulation, much remains to be learned about the protein phosphorylation and dephosphorylation reactions that underlie the regulation of the channels. The channel isoform most well studied biochemically is that expressed in skeletal muscle. The alpha 1- and beta-subunits of this channel isoform are substrates for protein kinase A, but it is unknown if phosphorylation or dephosphorylation of both subunits contributes to altered channel properties. Here, we report experiments in which the alpha 1- and beta-subunits were differentially phosphorylated by protein kinase A and dephosphorylated by protein phosphatase 1c under conditions that led to channel regulation. The results suggest that the alpha 1-subunit plays a key role in the phosphorylation and dephosphorylation-dependent regulation of the L-type Ca channels from skeletal muscle.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Zhao XL,Gutierrez LM,Chang CF,Hosey MMdoi
10.1006/bbrc.1994.1024subject
Has Abstractpub_date
1994-01-14 00:00:00pages
166-73issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(84)71024-2journal_volume
198pub_type
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