Molecular architecture of the complete COG tethering complex

Jun Yong Ha; Hui-Ting Chou; Daniel Ungar; Calvin K Yip; Thomas Walz; Frederick M Hughson

doi:10.1038/nsmb.3263

Molecular architecture of the complete COG tethering complex

Jun Yong Ha, Hui-Ting Chou, Daniel Ungar, Calvin K Yip, Thomas Walz, Frederick M Hughson

Biology

Research output: Contribution to journal › Article › peer-review

Abstract

The conserved oligomeric Golgi (COG) complex orchestrates vesicular trafficking to and within the Golgi apparatus. Here, we use negative-stain electron microscopy to elucidate the architecture of the hetero-octameric COG complex from Saccharomyces cerevisiae. Intact COG has an intricate shape, with four (or possibly five) flexible legs, that differs strikingly from that of the exocyst complex and appears to be well suited for vesicle capture and fusion.

Original language	English
Pages (from-to)	758-760
Number of pages	3
Journal	Nature Structural & Molecular Biology
Volume	23
DOIs	https://doi.org/10.1038/nsmb.3263
Publication status	Published - 18 Jul 2016

Bibliographical note

This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. Embargo period: 6 months [paper and supplementary file]

Keywords

Adaptor Proteins, Vesicular Transport/ultrastructure
Golgi Apparatus/ultrastructure
Microscopy, Electron
Multiprotein Complexes/ultrastructure
Protein Structure, Quaternary
Saccharomyces cerevisiae Proteins/ultrastructure
Saccharomyces cerevisiae/ultrastructure

Access to Document

10.1038/nsmb.3263

Ha et al. NSMB accepted version 2016
This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details
Accepted author manuscript, 2.97 MB

Cite this

@article{d5299b2067764bbc9527acdcb3a3b6b1,

title = "Molecular architecture of the complete COG tethering complex",

abstract = "The conserved oligomeric Golgi (COG) complex orchestrates vesicular trafficking to and within the Golgi apparatus. Here, we use negative-stain electron microscopy to elucidate the architecture of the hetero-octameric COG complex from Saccharomyces cerevisiae. Intact COG has an intricate shape, with four (or possibly five) flexible legs, that differs strikingly from that of the exocyst complex and appears to be well suited for vesicle capture and fusion.",

keywords = "Adaptor Proteins, Vesicular Transport/ultrastructure, Golgi Apparatus/ultrastructure, Microscopy, Electron, Multiprotein Complexes/ultrastructure, Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins/ultrastructure, Saccharomyces cerevisiae/ultrastructure",

author = "Ha, {Jun Yong} and Hui-Ting Chou and Daniel Ungar and Yip, {Calvin K} and Thomas Walz and Hughson, {Frederick M}",

note = "This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details. Embargo period: 6 months [paper and supplementary file] ",

year = "2016",

month = jul,

day = "18",

doi = "10.1038/nsmb.3263",

language = "English",

volume = "23",

pages = "758--760",

journal = "Nature Structural & Molecular Biology",

issn = "1545-9993",

publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Molecular architecture of the complete COG tethering complex

AU - Ha, Jun Yong

AU - Chou, Hui-Ting

AU - Ungar, Daniel

AU - Yip, Calvin K

AU - Walz, Thomas

AU - Hughson, Frederick M

N1 - This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. Embargo period: 6 months [paper and supplementary file]

PY - 2016/7/18

Y1 - 2016/7/18

N2 - The conserved oligomeric Golgi (COG) complex orchestrates vesicular trafficking to and within the Golgi apparatus. Here, we use negative-stain electron microscopy to elucidate the architecture of the hetero-octameric COG complex from Saccharomyces cerevisiae. Intact COG has an intricate shape, with four (or possibly five) flexible legs, that differs strikingly from that of the exocyst complex and appears to be well suited for vesicle capture and fusion.

AB - The conserved oligomeric Golgi (COG) complex orchestrates vesicular trafficking to and within the Golgi apparatus. Here, we use negative-stain electron microscopy to elucidate the architecture of the hetero-octameric COG complex from Saccharomyces cerevisiae. Intact COG has an intricate shape, with four (or possibly five) flexible legs, that differs strikingly from that of the exocyst complex and appears to be well suited for vesicle capture and fusion.

KW - Adaptor Proteins, Vesicular Transport/ultrastructure

KW - Golgi Apparatus/ultrastructure

KW - Microscopy, Electron

KW - Multiprotein Complexes/ultrastructure

KW - Protein Structure, Quaternary

KW - Saccharomyces cerevisiae Proteins/ultrastructure

KW - Saccharomyces cerevisiae/ultrastructure

UR - http://www.scopus.com/inward/record.url?scp=84978718885&partnerID=8YFLogxK

U2 - 10.1038/nsmb.3263

DO - 10.1038/nsmb.3263

M3 - Article

SN - 1545-9993

VL - 23

SP - 758

EP - 760

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

ER -

Molecular architecture of the complete COG tethering complex

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Dani Ungar

Protein Sorting, MC IRG: Vesicular protein sorting in the Golgi apparatus

Cite this

Molecular architecture of the complete COG tethering complex

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Profiles

Dani Ungar

Projects

Protein Sorting, MC IRG: Vesicular protein sorting in the Golgi apparatus

Cite this