Identification of RII-binding proteins in the mollusc Mytilus galloprovincialis.
Several proteins with M(r) > 70 kDa from various tissues of the sea mussel Mytilus galloprovincialis were specifically recognized in vitro by the regulatory subunit (type RII alpha) of cAMP-dependent protein kinase (cAPK) from porcine heart. However, none of these proteins interacted with the regulatory subunit of cAPK from the mollusc itself. The results suggest that, unlike mammalian RII, regulatory subunit from mussel lacks the specific residues responsible for interaction with R-binding proteins. Consequently, the identified molluscan RII alpha-binding proteins should play a distinct role from cAPK anchoring.
Cao
J
J
Departamento de Bioquímica e Bioloxía Molecular, Facultade de Veterinaria, Universidade de Santiago de Compostela, Lugo, Spain.
Fernández
M
M
Ramos-Martínez
J I
JI
Villamarín
J A
JA
D000818:Animals; D001483:Base Sequence; D049872:Bivalvia / Q000737:chemistry*; D002352:Carrier Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry; D000242:Cyclic AMP / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D003600:Cytosol / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009206:Myocardium / Q000737:chemistry; D011485:Protein Binding; D013552:Swine
D002352:Carrier Proteins; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases