Identification of RII‐binding proteins in the mollusc <i>Mytilus galloprovincialis</i>

Cao, Jesús; Fernández, Montserrat; Ramos-Martı́nez, Juan Ignacio; Villamarín, J. Antonio

doi:10.1016/0014-5793(96)00158-5

Cited by 10 publications

(1 citation statement)

References 30 publications

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“…Furthermore, the particular localization of the R myt2 isoform suggests that it may be associated with cellular structures and organella, through its interaction with anchoring proteins, like occurs with the RII-type subunit from mammals (Pawson and Scott 1997;Michel and Scott 2002). However, our attempts to identify these PKA-anchoring proteins in mantle extracts were so far unsuccessful (Cao et al 1996). In previous work we had been reported that R myt1 and R myt2 have specific structural and biochemical properties besides its common ability to inhibit the C-subunit in the absence of cAMP.…”

Section: Discussionmentioning

confidence: 90%

Differential distribution of cAMP-dependent protein kinase isoforms in the mantle of the bivalve mollusc Mytilus galloprovincialis

2009

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Two different isoforms of the regulatory (R) subunit of cAMP-dependent protein kinase (PKA), named R(myt1) and R(myt2), had previously been identified in the sea mussel Mytilus galloprovincialis. R(myt1) and R(myt2) were differentially distributed in the various cell types comprising the mussel mantle. R(myt1) was found the only isoform to be present in the auxiliary cells of female follicles and the cubic epithelium of the middle fold of mantle edge. In contrast, only the R(myt2) isoform was detected in the subepithelial connective tissue, the endothelium of haemolymph vessels, the adipogranular and vesicular cells of reserve connective tissue, and the spermatozoa. Finally, both R(myt1) and R(myt2) coexist in some cell types but they show a different cellular localization: R(myt1) was localized in the cytoplasm whereas R(myt2) was mainly detected in the cell apical edge, cell periphery, cilia and sperm flagella. Interestingly, both R(myt1) and R(myt2) were absent in oocytes within the female gonadal follicles but, in contrast, they were highly expressed in follicle-released oocytes collected after spawning. Taken together the results show that mussel PKA isoforms are differentially distributed in the mantle cell types, which suggests that they are involved in the regulation of distinct cellular functions. On the other hand, the expression of R(myt1) and R(myt2) proteins is associated with the meiosis resumption of oocytes at the prophase I stage, which occurs in parallel to spawning.

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Section: Discussionmentioning

confidence: 90%

Differential distribution of cAMP-dependent protein kinase isoforms in the mantle of the bivalve mollusc Mytilus galloprovincialis

2009

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Purification of a Novel Isoform of the Regulatory Subunit of cAMP-Dependent Protein Kinase from the Bivalve MolluskMytilus galloprovincialis

Rodriguez

Barcia

et al. 1998

Archives of Biochemistry and Biophysics

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Effects of the C-terminal peptide of the αs subunit of the G protein on the regulation of adenylyl cyclase and protein kinase A activities by biogenic amines and glucagon in mollusk and rat muscles

Korol'kov

Plesneva

et al. 2005

Neurosci Behav Physiol

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The C-terminal parts of the a subunits of heteromeric G proteins play an important role in the functional linkage of G proteins with receptors of the serpentine type. The present report describes studies of the effects of the C-terminal octapeptide 387-394 of the alphaS subunit of the mammalian G protein on the transmission of the hormonal signal via the hormone-sensitive adenylyl cyclase signal system, whose major components are receptors of the serpentine type, G proteins, and the enzymes adenylyl cyclase and protein kinase A. The peptide synthesized here, 387-394 amide (10(-7) - 10(-4) M), dose-dependently decreased adenylyl cyclase and protein kinase A activities stimulated by serotonin and glucagon in smooth muscle from the freshwater bivalve mollusk Anodonta cygnea and by the beta agonist isoproterenol in rat skeletal muscle. At a concentration as low as 10(-7) M, the peptide released potentiation of the stimulatory effects of hormones on adenylyl cyclase activity due to the non-hydrolyzable guanine nucleotide analog Gpp[NH]p. At the same time, it had almost no effect on the stimulation of adenylyl cyclase activity by non-hormonal agents (NaF, Gpp[NH]p, and forskolin). The inhibitory effects of hormones on adenylyl cyclase and protein kinase A activities persisted in the presence of the peptide. Our data demonstrate the importance of the C-terminal part of the alphaS subunit of the stimulatory G protein for its functional linkage with receptors of the serpentine type and throw light on the molecular mechanisms of the interactions between G proteins and receptors.

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Identification of RII‐binding proteins in the mollusc Mytilus galloprovincialis

Cited by 10 publications

References 30 publications

Differential distribution of cAMP-dependent protein kinase isoforms in the mantle of the bivalve mollusc Mytilus galloprovincialis

Differential distribution of cAMP-dependent protein kinase isoforms in the mantle of the bivalve mollusc Mytilus galloprovincialis

Purification of a Novel Isoform of the Regulatory Subunit of cAMP-Dependent Protein Kinase from the Bivalve MolluskMytilus galloprovincialis

Effects of the C-terminal peptide of the αs subunit of the G protein on the regulation of adenylyl cyclase and protein kinase A activities by biogenic amines and glucagon in mollusk and rat muscles

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