A Novel Muscle Protein Located inside the Terminal Cisternae of the Sarcoplasmic Reticulum

Presotto, Cristina; Agnolucci, Laura; Biral, Donatella; Dainese, Paola; Bernardi, Paolo; Salviati, G.

doi:10.1074/jbc.272.10.6534

Cited by 3 publications

(1 citation statement)

References 25 publications

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“…A protein of " 167 kDa apparent molecular mass was detected in skeletal and cardiac muscles, but not in other tissues, using an antiserum against α & β " -integrin [184]. This protein is biochemically and immunologically distinct from the integrins, has a unique N-terminal sequence, is highly enriched in the TC and is located intralumenally.…”

Section: Integrin-like Proteinmentioning

confidence: 95%

Protein–protein interactions in intracellular Ca2+-release channel function

Mackrill

1999

Biochemical Journal

143

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Release of Ca2+ ions from intracellular stores can occur via two classes of Ca2+-release channel (CRC) protein, the inositol 1,4, 5-trisphosphate receptors (InsP3Rs) and the ryanodine receptors (RyRs). Multiple isoforms and subtypes of each CRC class display distinct but overlapping distributions within mammalian tissues. InsP3Rs and RyRs interact with a plethora of accessory proteins which modulate the activity of their intrinsic channels. Although many aspects of CRC structure and function have been reviewed in recent years, the properties of proteins with which they interact has not been comprehensively surveyed, despite extensive current research on the roles of these modulators. The aim of this article is to review the regulation of CRC activity by accessory proteins and, wherever possible, to outline the structural details of such interactions. The CRCs are large transmembrane proteins, with the bulk of their structure located cytoplasmically. Intra- and inter-complex protein-protein interactions between these cytoplasmic domains also regulate CRC function. Some accessory proteins modulate channel activity of all CRC subtypes characterized, whereas other have class- or even isoform-specific effects. Certain accessory proteins exert both direct and indirect forms of regulation on CRCs, occasionally with opposing effects. Others are themselves modulated by changes in Ca2+ concentration, thereby participating in feedback mechanisms acting on InsP3R and RyR activity. CRCs are therefore capable of integrating numerous signalling events within a cell by virtue of such protein-protein interactions. Consequently, the functional properties of InsP3Rs and RyRs within particular cells and subcellular domains are 'customized' by the accessory proteins present.

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Section: Integrin-like Proteinmentioning

confidence: 95%

Protein–protein interactions in intracellular Ca2+-release channel function

Mackrill

1999

Biochemical Journal

143

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EHD proteins are associated with tubular and vesicular compartments and interact with specific phospholipids

Blume¹,

Halbach²,

Behrendt³

et al. 2007

Experimental Cell Research

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Exciting perspectives for Translational Myology in the Abstracts of the 2018Spring PaduaMuscleDays: Giovanni Salviati Memorial – Chapter I - Foreword

Carraro

2018

Eur J Transl Myol

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Myologists working in Padua (Italy) were able to continue a half-century tradition of studies of skeletal muscles, that started with a research on fever, specifically if and how skeletal muscle contribute to it by burning bacterial toxin. Beside main publications in high-impact-factor journals by Padua myologists, I hope to convince readers (and myself) of the relevance of the editing Basic and Applied Myology (BAM), retitled from 2010 European Journal of Translational Myology (EJTM), of the institution of the Interdepartmental Research Center of Myology of the University of Padova (CIR-Myo), and of a long series of International Conferences organized in Euganei Hills and Padova, that is, the PaduaMuscleDays. The 2018Spring PaduaMuscleDays (2018SpPMD), were held in Euganei Hills and Padua (Italy), in March 14-17, and were dedicated to Giovanni Salviati. The main event of the “Giovanni Salviati Memorial”, was held in the Aula Guariento, Accademia Galileiana di Scienze, Lettere ed Arti of Padua to honor a beloved friend and excellent scientist 20 years after his premature passing. Using the words of Prof. Nicola Rizzuto, we all share his believe that Giovanni “will be remembered not only for his talent and originality as a biochemist, but also for his unassuming and humanistic personality, a rare quality in highly successful people like Giovanni. The best way to remember such a person is to gather pupils and colleagues, who shared with him the same scientific interests and ask them to discuss recent advances in their own fields, just as Giovanni have liked to do”. Since Giovanni’s friends sent many abstracts still influenced by their previous collaboration with him, all the Sessions of the 2018SpPMD reflect both to the research aims of Giovanni Salviati and the traditional topics of the PaduaMuscleDays, that is, basics and applications of physical, molecular and cellular strategies to maintain or recover functions of skeletal muscles. The translational researches summarized in the 2018SpPMD Abstracts are at the appropriate high level to attract approval of Ethical Committees, the interest of International Granting Agencies and approval for publication in top quality, international journals. This was true in the past, continues to be true in the present and will be true in the future. All 2018SpPMD Abstracts are indexed at the end of the Chapter IV.

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A Novel Muscle Protein Located inside the Terminal Cisternae of the Sarcoplasmic Reticulum

Cited by 3 publications

References 25 publications

Protein–protein interactions in intracellular Ca2+-release channel function

Protein–protein interactions in intracellular Ca2+-release channel function

EHD proteins are associated with tubular and vesicular compartments and interact with specific phospholipids

Exciting perspectives for Translational Myology in the Abstracts of the 2018Spring PaduaMuscleDays: Giovanni Salviati Memorial – Chapter I - Foreword

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