The regulatory subunit of cAPK from mussels lacks specific residues for interaction with R-binding proteins, suggesting these proteins have a distinct role from cAPK anchoring in molluscs.
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Species differences in cAPK regulatory interactions caution against assuming conserved anchoring; leaves open distinct roles for these mussel proteins in invertebrates.
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.
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Cao et al. (1996) studied this question.
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