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  In situ structural analysis of Golgi intracisternal protein arrays

Engel, B. D., Schaffer, M., Albert, S., Asano, S., Plitzko, J. M., & Baumeister, W. (2015). In situ structural analysis of Golgi intracisternal protein arrays. Proceedings of the National Academy of Sciences of the United States of America, 112(36), 11264-11269. doi:10.1073/pnas.1515337112.

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 Creators:
Engel, Benjamin D.1, Author              
Schaffer, Miroslava1, Author              
Albert, Sahradha1, Author              
Asano, Shoh1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, 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: SCHERFFELIA-DUBIA PRASINOPHYCEAE; CHLAMYDOMONAS CELL-WALL; CRYOELECTRON TOMOGRAPHY; ELECTRON TOMOGRAPHY; APPARATUS ACTIVITY; VITREOUS SECTIONS; SCALE BIOGENESIS; EUKARYOTIC CELLS; MEMBRANE FLOW; POLYPHOSPHATEfocused ion beam; cryo-electron tomography; Chlamydomonas; Golgi; glycosyltransferase;
 Abstract: We acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo-electron tomography. These tomograms revealed structures within the Golgi cisternae that have not been seen before. Narrow trans-Golgi lumina were spanned by asymmetric membrane-associated protein arrays that had similar to 6-nm lateral periodicity. Subtomogram averaging showed that the arrays may determine the narrow central spacing of the trans-Golgi cisternae through zipper-like interactions, thereby forcing cargo to the trans-Golgi periphery. Additionally, we observed dense granular aggregates within cisternae and intracisternal filament bundles associated with trans-Golgi buds. These native in situ structures provide new molecular insights into Golgi architecture and function.

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Language(s): eng - English
 Dates: 2015-08-262015
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000360994900045
DOI: 10.1073/pnas.1515337112
 Degree: -

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Project name : Toxic Protein AGgregation in Neurodegeneration (ToPAG) ERC-2012-SyG
Grant ID : 318987
Funding program : Funding Programme 7 (FP7)
Funding organization : European Commission (EC)

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 112 (36) Sequence Number: - Start / End Page: 11264 - 11269 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230