Characterization of the junctional face membrane from terminal cisternae of sarcoplasmic reticulum.

Costello, Brian; Chadwick, Christopher C.; Saito, A; Chu, Alice; Maurer, Andreas; Fleischer, Sidney

doi:10.1083/jcb.103.3.741

Cited by 112 publications

(86 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The transverse tubules (Ttubules) are invaginations of the plasma membrane and contain the voltage sensing dihydropyridine receptor (DHPR). The portion of the SR terminal cisternae membrane facing the T-tubules is called junctional face membrane and contains the ryanodine receptor Ca 2+ release channel (RyR1), regulatory and structural proteins such as JP-45, triadin and junctin as well as a number of other proteins that are part of the RyR1 Ca 2+ release channel macromolecular structure [1][2][3][4]. In skeletal muscle, the triad, i.e.…”

Section: The Sarcoplasmic Reticulum and Ca 2+ Regulationmentioning

confidence: 99%

Ca2+ handling abnormalities in early-onset muscle diseases: Novel concepts and perspectives

Treves

Jungbluth

Voermans

et al. 2017

Seminars in Cell & Developmental Biology

View full text Add to dashboard Cite

a b s t r a c tThe physiological process by which Ca 2+ is released from the sarcoplasmic reticulum is called excitationcontraction coupling; it is initiated by an action potential which travels deep into the muscle fiber where it is sensed by the dihydropyridine receptor, a voltage sensing L-type Ca 2+ channel localized on the transverse tubules. Voltage-induced conformational changes in the dihydropyridine receptor activate the ryanodine receptor Ca 2+ release channel of the sarcoplasmic reticulum. The released Ca 2+ binds to troponin C, enabling contractile thick-thin filament interactions. The Ca 2+ is subsequently transported back into the sarcoplasmic reticulum by specialized Ca 2+ pumps (SERCA), preparing the muscle for a new cycle of contraction. Although other proteins are involved in excitation-contraction coupling, the mechanism described above emphasizes the unique role played by the two Ca 2+ channels (the dihydropyridine receptor and the ryanodine receptor), the SERCA Ca 2+ pumps and the exquisite spatial organization of the membrane compartments endowed with the proteins responsible for this mechanism to function rapidly and efficiently. Research over the past two decades has uncovered the fine details of excitation-contraction coupling under normal conditions while advances in genomics have helped to identify mutations in novel genes in patients with neuromuscular disorders. While it is now clear that many patients with congenital muscle diseases carry mutations in genes encoding proteins directly involved in Ca 2+ homeostasis, it has become apparent that mutations are also present in genes encoding for proteins not thought to be directly involved in Ca 2+ regulation. Ongoing research in the field now focuses on understanding the functional effect of individual mutations, as well as understanding the role of proteins not specifically located in the sarcoplasmic reticulum which nevertheless are involved in Ca 2+ regulation or excitation-contraction coupling. The principal challenge for the future is the identification of drug targets that can be pharmacologically manipulated by small molecules, with the ultimate aim to improve muscle function and quality of life of patients with congenital muscle disorders. The aim of this review is to give an overview of the most recent findings concerning Ca 2+ dysregulation and its impact on muscle function in patients with congenital muscle disorders due to mutations in proteins involved in excitation-contraction coupling and more broadly on Ca 2+ homeostasis.

show abstract

Section: The Sarcoplasmic Reticulum and Ca 2+ Regulationmentioning

confidence: 99%

Ca2+ handling abnormalities in early-onset muscle diseases: Novel concepts and perspectives

Treves

Jungbluth

Voermans

et al. 2017

Seminars in Cell & Developmental Biology

View full text Add to dashboard Cite

show abstract

“…Using these vesicles as starting material, CSQ was purified as described (Cala and Jones, 1983). Junctional face membranes (JFM) were isolated as reported elsewhere (Costello et al, 1986), with some minor modifications. Briefly, Triton X-100 was added at a final concentration of 0.5% to vesicles preincubated at 4ºC for 10 min in a solution containing 0.3 M sucrose, 1 mM CaCl 2 , 20 mM MOPS-Tris, pH 6.8.…”

Section: Isolation Proceduresmentioning

confidence: 99%

Fast kinetics of calcium dissociation from calsequestrin

2006

View full text Add to dashboard Cite

We measured the kinetics of calcium dissociation from calsequestrin in solution or forming part of isolated junctional sarcoplasmic reticulum membranes by mixing calsequestrin equilibrated with calcium with calcium-free solutions in a stopped-flow system. In parallel, we measured the kinetics of the intrinsic fluorescence changes that take place following calcium dissociation from calsequestrin. We found that at 25ºC calcium dissociation was 10-fold faster for calsequestrin attached to junctional membranes (k = 109 s -1 ) than in solution. These results imply that calcium dissociation from calsequestrin in vivo is not rate limiting during excitation-contraction coupling. In addition, we found that the intrinsic fluorescence decrease for calsequestrin in solution or forming part of junctional membranes was significantly slower than the rates of calcium dissociation. The kinetics of intrinsic fluorescence changes had two components for calsequestrin associated to junctional membranes and only one for calsequestrin in solution; the faster component was 8-fold faster (k = 54.1 s -1 ) than the slower component (k = 6.9 s -1 ), which had the same k value as for calsequestrin in solution. These combined results suggest that the presence of calsequestrin at high concentrations in a restricted space, such as when bound to the junctional membrane, accelerates calcium dissociation and the resulting structural changes, presumably as a result of cooperative molecular interactions.

show abstract

“…Such a result implies that the molecular machinery responsible for EC coupling comprises several protein components whose identification and functional role has yet to be defined. The anatomical site of skeletal-muscle EC coupling is the triad (TR), a unique intracellular synapse formed by the association of two membrane compartments : transverse tubules, which are an invagination of the sarcolemma and the sarcoplasmic-reticulum (SR) terminal cisternae (TC) [4,5]. The portion of TC facing the transverse tubules is called junctional-face membrane (JFM) SR [5].…”

Section: Introductionmentioning

confidence: 99%

“…The anatomical site of skeletal-muscle EC coupling is the triad (TR), a unique intracellular synapse formed by the association of two membrane compartments : transverse tubules, which are an invagination of the sarcolemma and the sarcoplasmic-reticulum (SR) terminal cisternae (TC) [4,5]. The portion of TC facing the transverse tubules is called junctional-face membrane (JFM) SR [5]. Ordered arrays of junctional feet, referable to as ' ryanodinereceptor Ca# + -release channel ' (RYR), bridge the gap of 9-12 nm Abbreviations used : EDL, extensor digitorum longus ; H(SR), (heavy) sarcoplasmic reticulum ; JFM, junctional-face membrane ; JFP, junctional face protein ; RYR, ryanodine-receptor Ca 2 + -release channel ; SOL, soleus ; TA, tibialis anterior ; TC, terminal cisternae ; EC, excitation-contraction ; DTT, dithiothreitol ; NCBI, National Center for Biotechnology Information ; KLH, keyhole-limpet haemocyanin ; TR, triad.…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane

Zorzato

Anderson

Ohlendieck

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

Using a biochemical/immunological approach to analyse the protein constituents of skeletal-muscle junctional-face membrane (JFM), we identified a 45kDa protein. Its N-terminal amino acid was blocked, but the amino acid sequence obtained from several peptides after proteolytic treatment did not significantly match that of any protein present in the SwissProt and NCBI (National Center for Biotechnology Information) databases. We synthesized a peptide whose sequence matched that of one of the peptides obtained after CNBr cleavage of the 45kDa protein; the peptide was conjugated to a carrier and used to raise antibodies. The antiserum was used to study in more detail the biochemical characteristics of the novel 45kDa protein. Analysis of the proteins present in different subcellular membrane fractions show that the novel 45kDa polypeptide: (i) is an integral membrane constituent present both in neonatal and adult skeletal-muscle sarcoplasmic reticulum; (ii) is selectively localized in the JFM; (iii) is not present in microsomes obtained from rabbit heart, liver or kidney. Immunoprecitation with anti-(45kDa protein) antibody indicates that the 45kDa protein is part of a complex which can be phosphorylated in vitro by the catalytic subunit of protein kinase A.

show abstract

Characterization of the junctional face membrane from terminal cisternae of sarcoplasmic reticulum.

Cited by 112 publications

References 40 publications

Ca2+ handling abnormalities in early-onset muscle diseases: Novel concepts and perspectives

Ca2+ handling abnormalities in early-onset muscle diseases: Novel concepts and perspectives

Fast kinetics of calcium dissociation from calsequestrin

Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane

Contact Info

Product

Resources

About