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In situ structural analysis of Golgi intracisternal protein arrays.
Proc. Natl. Acad. Sci. U.S.A. 112, 11264-11269 (2015)
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 ∼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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Chlamydomonas ; Golgi ; Cryo-electron Tomography ; Focused Ion Beam ; Glycosyltransferase
Language
english
Publication Year
2015
HGF-reported in Year
2015
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Volume: 112,
Issue: 36,
Pages: 11264-11269
Publisher
National Academy of Sciences
Reviewing status
Peer reviewed
Institute(s)
Helmholtz Pioneer Campus (HPC)
PubMed ID
26311849
Erfassungsdatum
2019-12-09