Cao J, Fernández M, Ramos-Martínez J I, Villamarín J A
Departamento de Bioquímica e Bioloxía Molecular, Facultade de Veterinaria, Universidade de Santiago de Compostela, Lugo, Spain.
FEBS Lett. 1996 Mar 11;382(1-2):93-6. doi: 10.1016/0014-5793(96)00158-5.
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.
来自地中海贻贝不同组织的几种分子量大于70 kDa的蛋白质,在体外被猪心脏的环磷酸腺苷依赖性蛋白激酶(cAPK)调节亚基(RIIα型)特异性识别。然而,这些蛋白质均不与贻贝自身的cAPK调节亚基相互作用。结果表明,与哺乳动物的RII不同,贻贝的调节亚基缺乏与R结合蛋白相互作用的特定残基。因此,所鉴定的贻贝RIIα结合蛋白应发挥与cAPK锚定不同的作用。