N-Myristoylation of the catalytic subunit of cAMP-dependent protein kinase in the free-living nematode Caenorhabditis elegans.
N-Myristoylation of the catalytic subunit (C-subunit) of cAMP-dependent protein kinase is widespread in animal cells. Some invertebrates express non-myristoylated isoforms of C-subunit but these co-exist with at least one myristoylated isoform. The generality of this observation implies an indispensable function for myristoylated C-subunit, but notwithstanding this, neither of the C-subunit isoforms hitherto described in C. elegans is apparently N-myristoylated. In light of this anomaly, the myristoylation status of the C-subunit has been examined in adult C. elegans. Evidence is presented for the presence of an N-myristoylated isoform.
Aspbury
R A
RA
Department of Biochemistry, University of Liverpool, Liverpool, L69 3BX, United Kingdom.
Fisher
M J
MJ
Rees
H H
HH
Clegg
R A
RA
D000818:Animals; D017173:Caenorhabditis elegans; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D009226:Myristates
D009226:Myristates; D017868:Cyclic AMP-Dependent Protein Kinases