Co-localization of the dihydropyridine receptor and the cyclic AMP-binding subunit of an intrinsic protein kinase to the junctional membrane of the transverse tubules of skeletal muscle

Salvatori, Sergio; Damiani, Ernesto; Barhanin, Jacques; Furlan, Sandra; Salviati, G.; Margreth, Alfredo

doi:10.1042/bj2670679

Cited by 33 publications

(17 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results on skeletal muscles have shown that the pump of rabbit fast-twitch muscle localized to the same membrane domain of the transverse tubules to which the dihydropyridine receptor was confined, i.e., to the junctional membrane (Salvatori et al, 1990). In agreement with these findings, PMCA remained bound to the junctional-transverse-tubule component on dissociation of the isolated triads from rabbit skeletal muscles.…”

Section: Y Isupporting

confidence: 70%

“…Studies on rabbit fast-twitch muscle (Salvatori et al, 1990) have shown that junctional transverse tubules differ from free transverse tubules, since they have a very high density of highaffinity dihydropyridine-binding sites. The latter are specifically located at the junctional domain of the transverse tubules, in the gap between the transverse tubules and the terminal cisternae of the SR.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Colocalization of the Dihydropyridine Receptor, the Plasma‐Membrane Calcium ATPase Isoform 1 and the Sodium/Calcium Exchanger to the Junctional‐Membrane Domain of Transverse Tubules of Rabbit Skeletal Muscle

Sacchetto

Margreth

Pelosi

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

The subcellular distribution of the calmodulin-stimulated plasma-membrane Ca*+-ATPase (PMCA) has been studied in rat and rabbit skeletal muscle cells by indirect (calmodulin gel overlays) and direct (Western blotting with specific antibodies) methods. It has also been studied in situ in immunocytochemistry experiments. The distribution of PMCA has been compared with that of the Na+/Ca*+ exchanger and of the dihydropyridine receptor, which has been studied by Western blotting with specific antibodies. Both PMCA and the Na+/Ca'+ exchanger had a dual localization, i.e., they were found in the plasma membrane and in the transverse-tubule fractions of the two main types of skeletal muscles studied. The pump and the exchanger were not diffusely distributed in the transverse-tubule-membrane system, but specifically confined to the membrane domain where the dihydropyridine receptor was also localized, i.e., the junctional membrane. Experiments with isoform-specific antibodies have shown that the pump isoform expressed in skeletal muscle is PMCA 1.

show abstract

Section: Y Isupporting

confidence: 70%

Section: Resultsmentioning

confidence: 99%

Colocalization of the Dihydropyridine Receptor, the Plasma‐Membrane Calcium ATPase Isoform 1 and the Sodium/Calcium Exchanger to the Junctional‐Membrane Domain of Transverse Tubules of Rabbit Skeletal Muscle

Sacchetto

Margreth

Pelosi

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Previous evidence for a physical association between PKA and the L-type Ca2+ channel has come from biochemical experiments in which kinase copurifies with the channel in partially purified preparations (30,31). In our experiments, a synthetic peptide representing residues 493-515 ofthe human thyroid AKAP, Ht 31 (23), was found to block kinasedependent potentiation in both mouse and rabbit skeletal muscle myotubes.…”

Section: Discussionmentioning

confidence: 53%

Voltage-dependent potentiation of L-type Ca2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein kinase.

Johnson

Scheuer

Catterall

1994

Proc. Natl. Acad. Sci. U.S.A.

177

114

View full text Add to dashboard Cite

Skeletal muscle L-type Ca2+ channels in the transverse tubule membrane play critical roles in initiating contraction and in regulating Ca2+ entry (1). A voltage-driven conformational change in the al subunit ofthis Ca2+ channel is thought to trigger the release ofCa2+ from the sarcoplasmic reticulum (2, 3) via protein-protein interactions at the transverse tubule-sarcoplasmic reticulum junction (4-6). The resulting Ca2+ release through the sarcoplasmic reticulum Ca2+ channel initiates contraction (7).The Ca2+ conductance ofthe skeletal muscle Ca2+ channel activates slowly, and only a small fraction of the channels open simultaneously during a single depolarizing stimulus (8).Trains of prepulses to positive membrane potentials that mimic action potentials greatly increase Ca2+ current in response to a subsequent depolarization (9). This Ca2+ channel potentiation is due to rapid phosphorylation by cAMPdependent protein kinase (PKA) at positive membrane potentials and results in a negative shift in the voltage dependence of channel activation and slowing of channel deactivation. Potentiation is reversed within seconds at repolarized membrane potentials by the action of phosphoprotein phosphatases. The force of vertebrate skeletal muscle contraction is substantially increased in response to highfrequency stimulation (10), and this effect is dependent upon extracellular Ca2+ and on the ion-conductance activity of L-type Ca2+ channels (11-13). We have hypothesized that increased contractile force may result from the increased Ca2+ entry through L-type Ca2+ channels whose activity is potentiated by voltage-dependent phosphorylation during and following depolarization (9). This increased Ca2+ entry would increase the store of Ca2+ for release from the sarcoplasmic reticulum during subsequent action potentials. Similar L-type Ca2+ channel potentiation by depolarizing prepulses is observed in cardiac myocytes (14-18) and chromaffin cells (19) and also involves voltage-dependent protein phosphorylation (19,20).A surprising feature of skeletal muscle Ca2+ channel potentiation by voltage-dependent PKA phosphorylation is its rapid response time; 200-Hz trains of positive prepulses as short as 3 msec are effective in potentiating Ca2+ channel activity (9). Many PKA-mediated events occur on a time scale of seconds because of concentration and diffusion limits. PKA is a soluble protein consisting of a central dimer ofregulatory subunits with two associated catalytic subunits. Binding of cAMP to the regulatory subunits reversibly releases active catalytic subunits (21,22). The RII regulatory subunit of PKA also binds to PKA-anchoring proteins (AKAPs) through a conserved binding domain (23), which can be disrupted by a 24-amino acid region from a human thyroid AKAP, Ht 31. Ht 31 peptide prevents RII-AKAP binding in most tissues and disrupts phosphorylation required for the basal activity of the a-amino-3-hydroxy-5-methyl4 isoxazolepropionic acid (AMPA)/kainate receptors in hippocampal neurons (24). This interaction occurs ...

show abstract

“…[␣- 32 P]ATP Photoaffinity Labeling-Photoaffinity labeling was carried out by the UV irradiation method previously described (25). Dystrophin-DAPs preparations (14 -21 g of protein) or sarcolemma membranes (28 g of protein) were equilibrated with 0.4 M ATP (containing 2 and 4 Ci of [␣-32 P]ATP, respectively) in 100 l of the following different assay environments: 1) Ca-Mg buffer: 25 mM Tris, pH 7.4, 2.5 mM MgCl 2 , 10 M CaCl 2 , and 1 mM dithiothreitol; 2) magnesium buffer: 25 mM Tris, pH 7.4, 2.5 mM MgCl 2 , 2.5 mM EGTA, and 1 mM dithiothreitol; 3) Ca/Mg-free buffer: 25 mM Tris, pH 7.4, 2.5 mM EGTA, 2.5 mM EDTA, and 1 mM dithiothreitol.…”

mentioning

confidence: 99%

Ecto-ATPase Activity of α-Sarcoglycan (Adhalin)

Betto¹,

Senter

Ceoldo

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

␣-Sarcoglycan is a component of the sarcoglycan complex of dystrophin-associated proteins. Mutations of any of the sarcoglycan genes cause specific forms of muscular dystrophies, collectively termed sarcoglycanopathies. Importantly, a deficiency of any specific sarcoglycan affects the expression of the others. Thus, it appears that the lack of sarcoglycans deprives the muscle cell of an essential, yet unknown function. In the present study, we provide evidence for an ecto-ATPase activity of ␣-sarcoglycan. ␣-Sarcoglycan binds ATP in a Mg Dystrophin is a large cytoskeletal protein associated with a complex of integral and peripheral membrane proteins collectively termed DAPs.1 Dystrophin is a long filamentous protein comprising four distinct structural domains: the amino-terminal domain, which binds F-actin, the rod-like central domain; the cysteine-rich domain, which binds the cytoplasmic portion of ␤-dystroglycan and syntrophins; and the carboxyl-terminal domain (1). The DAPs complex is composed of three subcomplexes: syntrophins, dystroglycans, and sarcoglycans (2, 3). Syntrophins are peripheral membrane proteins of unknown function that bind the carboxyl terminus of dystrophin (4, 5). Dystroglycans consist of two proteins derived from a common precursor protein: ␣-dystroglycan, a peripheral glycoprotein that binds extracellular matrix proteins like laminin-2 (merosin) and, in the neuromuscular junction, laminin-4 (agrin); and ␤-dystroglycan, an intrinsic membrane protein that binds dystrophin at its cytoplasmic tail and ␣-dystroglycan at the opposite end (6, 7). Therefore, the dystroglycans represent the link between the subsarcolemmal actin cytoskeleton and the extracellular matrix through dystrophin. Five sarcoglycans have been described: ␣-sarcoglycan (adhalin, 50 kDa), ␤-sarcoglycan (43 kDa), ␥-and ␦-sarcoglycans (35 kDa) (8 -10), and ⑀-sarcoglycan (11, 12). The function of the sarcoglycans remains unknown.Dystrophin is defective in Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy. In patients with DMD and in the mdx mouse, an animal model for DMD, all of the components of the DAPs are severely reduced at the sarcolemma (13, 14), even though they are almost normal at the neuromuscular junction (15).Mutations in the ␣-sarcoglycan gene, which is located on chromosome 17q21 (10), were demonstrated in limb girdle muscular dystrophy-2D (LGMD-2D), an autosomal recessive muscular dystrophy that affects both females and males (16,17). In LGMD-2D, ␤-and ␥-sarcoglycan were also absent or greatly reduced, whereas dystrophin and the dystroglycan complex were preserved (18). Similar modifications were also found in the skeletal muscle of the cardiomyopatic hamster, an animal model of this disease (19). Recently, mutations in the genes that encode for ␤-, ␥-, and ␦-sarcoglycan, located on chromosomes 4q12, 13q12, and 5q33-34, were discovered in LGMD-2E, -2C, and -2F, respectively (9,20,21). These mutations caused the absence not only of the respective protein product but also of the other three components...

show abstract

Co-localization of the dihydropyridine receptor and the cyclic AMP-binding subunit of an intrinsic protein kinase to the junctional membrane of the transverse tubules of skeletal muscle

Cited by 33 publications

References 60 publications

Colocalization of the Dihydropyridine Receptor, the Plasma‐Membrane Calcium ATPase Isoform 1 and the Sodium/Calcium Exchanger to the Junctional‐Membrane Domain of Transverse Tubules of Rabbit Skeletal Muscle

Colocalization of the Dihydropyridine Receptor, the Plasma‐Membrane Calcium ATPase Isoform 1 and the Sodium/Calcium Exchanger to the Junctional‐Membrane Domain of Transverse Tubules of Rabbit Skeletal Muscle

Voltage-dependent potentiation of L-type Ca2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein kinase.

Ecto-ATPase Activity of α-Sarcoglycan (Adhalin)

Contact Info

Product

Resources

About