このエントリーをはてなブックマークに追加
ID 57390
FullText URL
Author
Satoh, Ayano Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University ORCID Kaken ID publons
Hayashi-Nishino, Mitsuko Institute of Scientific and Industrial Research, Osaka University
Shakuno, Takuto Graduate School of Natural Science and Technology, Okayama University
Masuda, Junko Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University
Koreishi, Mayuko Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University
Murakami, Runa Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University
Nakamura, Yoshimasa raduate School of Environmental and Life Science, Okayama University ORCID Kaken ID publons researchmap
Nakamura, Toshiyuki raduate School of Environmental and Life Science, Okayama University
Abe-Kanoh, Naomi raduate School of Environmental and Life Science, Okayama University
Honjo, Yasuko esearch Institute for Radiation Biology and Medicine, Hiroshima University
Malsam, Joerg Center for Biochemistry (BZH), Heidelberg University
Yu, Sidney School of Biomedical Sciences, The Chinese University of Hong Kong
ishino, Kunihiko Institute of Scientific and Industrial Research, Osaka University
Abstract
Golgins are a family of Golgi-localized long coiled-coil proteins. The major golgin function is thought to be the tethering of vesicles, membranes, and cytoskeletal elements to the Golgi. We previously showed that knockdown of one of the longest golgins, Giantin, altered the glycosylation patterns of cell surfaces and the kinetics of cargo transport, suggesting that Giantin maintains correct glycosylation through slowing down transport within the Golgi. Giantin knockdown also altered the sizes and numbers of mini Golgi stacks generated by microtubule de-polymerization, suggesting that it maintains the independence of individual Golgi stacks. Therefore, it is presumed that Golgi stacks lose their independence following Giantin knockdown, allowing easier and possibly increased transport among stacks and abnormal glycosylation. To gain structural insights into the independence of Golgi stacks, we herein performed electron tomography and 3D modeling of Golgi stacks in Giantin knockdown cells. Compared with control cells, Giantin-knockdown cells had fewer and smaller fenestrae within each cisterna. This was supported by data showing that the diffusion rate of Golgi membrane proteins is faster in Giantin-knockdown Golgi, indicating that Giantin knockdown structurally and functionally increases connectivity among Golgi cisternae and stacks. This increased connectivity suggests that contrary to the cis-golgin tether model, Giantin instead inhibits the tether and fusion of nearby Golgi cisternae and stacks, resulting in transport difficulties between stacks that may enable the correct glycosylation of proteins and lipids passing through the Golgi.
Keywords
Golgi
golgins
glycosylation
endoplasmic reticulum
electron tomography
Published Date
2019-08-27
Publication Title
Frontiers in Cell and Developmental Biology
Volume
volume7
Start Page
160
ISSN
2296634X
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
File Version
publisher
PubMed ID
DOI
Related Url
isVersionOf https://doi.org/10.3389/fcell.2019.00160
Citation
Satoh A, Hayashi-Nishino M, Shakuno T, Masuda J, Koreishi M, Murakami R, Nakamura Y, Nakamura T, Abe-Kanoh N, Honjo Y, Malsam J, Yu S and Nishino K (2019) The Golgin Protein Giantin Regulates Interconnections Between Golgi Stacks. Front. Cell Dev. Biol. 7:160. doi: 10.3389/fcell.2019.00160