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  Supramolecular architecture of endoplasmic reticulum - plasma membrane contact sites

Fernandez-Busnadiego, R. (2016). Supramolecular architecture of endoplasmic reticulum - plasma membrane contact sites. Biochemical Society Transactions (London), 44, 534-540. doi:10.1042/BST20150279.

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Fernandez-Busnadiego, Ruben1, Author              
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1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: SKELETAL-MUSCLE; RYANODINE RECEPTOR; ORP/OSH PROTEINS; CALCIUM-CHANNELS; CELLS; JUNCTIONS; HEART; TOMOGRAPHY; REVEALS; DRIVENBiochemistry & Molecular Biology; cryo-EM; extended-synaptotagmin; lipid transfer; Orai; ryanodine receptor; STIM;
 Abstract: The endoplasmic reticulum (ER) forms membrane contact sites (MCS) with most other cellular organelles and the plasma membrane (PM). These ER-PM MCS, where the membranes of the ER and PM are closely apposed, were discovered in the early days of electron microscopy (EM), but only recently are we starting to understand their functional and structural diversity. ER-PM MCS are nowadays known to mediate excitation-contraction coupling (ECC) in striated muscle cells and to play crucial roles in Ca2+ and lipid homoeostasis in all metazoan cells. A common feature across ER-PM MCS specialized in different functions is the preponderance of cooperative phenomena that result in the formation of large supramolecular assemblies. Therefore, characterizing the supramolecular architecture of ER-PM MCS is critical to understand their mechanisms of function. Cryo-electron tomography (cryo-ET) is a powerful EM technique uniquely positioned to address this issue, as it allows 3D imaging of fully hydrated, unstained cellular structures at molecular resolution. In this review I summarize our current structural knowledge on the molecular organization of ER-PM MCS and its functional implications, with special emphasis on the emerging contributions of cryo-ET.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000377518000031
DOI: 10.1042/BST20150279
 Degree: -

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Title: Biochemical Society Transactions (London)
  Other : Biochem Soc Trans
Source Genre: Journal
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Publ. Info: London : Portland Press.
Pages: - Volume / Issue: 44 Sequence Number: - Start / End Page: 534 - 540 Identifier: ISSN: 0300-5127
CoNE: https://pure.mpg.de/cone/journals/resource/954925507337