Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0138789
Title: The ubiquitin ligase CBLC maintains the network organization of the Golgi apparatus
Authors: Lee W.Y.
Goh G.
Chia J.
Boey A.
Gunko N.V.
Bard F. 
Keywords: Cbl protein
CBLC protein
ligase
protein tyrosine kinase
RING finger protein
unclassified drug
Cbl protein
green fluorescent protein
protein tyrosine kinase
Article
controlled study
down regulation
electron microscopy
enzyme activation
enzyme activity
enzyme localization
Golgi complex
human
human cell
protein degradation
protein depletion
protein domain
protein function
protein protein interaction
regulatory mechanism
ubiquitination
confocal microscopy
genetics
HeLa cell line
immunoblotting
metabolism
mutation
RNA interference
trans Golgi network
tumor cell line
ultrastructure
Cell Line, Tumor
Green Fluorescent Proteins
HeLa Cells
Humans
Immunoblotting
Microscopy, Confocal
Microscopy, Electron
Mutation
Proto-Oncogene Proteins c-cbl
RNA Interference
src-Family Kinases
trans-Golgi Network
Issue Date: 2015
Publisher: Public Library of Science
Citation: Lee W.Y., Goh G., Chia J., Boey A., Gunko N.V., Bard F. (2015). The ubiquitin ligase CBLC maintains the network organization of the Golgi apparatus. PLoS ONE 10 (9) : e0138789. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0138789
Abstract: The Golgi apparatus plays a pivotal role in the sorting and post-translational modifications of secreted and membrane proteins. In mammalian cells, the Golgi is organized in stacks of cisternae linked together to form a network with a ribbon shape. Regulation of Golgi ribbon formation is poorly understood. Here we find in an image-based RNAi screen that depletion of the ubiquitin-ligase CBLC induces Golgi fragmentation. Depletions of the close homologues CBL and CBLB do not induce any visible defects. In CBLC-depleted cells, Golgi stacks appear relatively unperturbed at both the light and electron microscopy levels, suggesting that CBLC controls mostly network organization. CBLC partially localizes on Golgi membranes and this localization is enhanced after activation of the SRC kinase. Inhibition of SRC reverts CBLC depletion effects, suggesting interplay between the two. CBLC's regulation of Golgi network requires its ubiquitin ligase activity. However, SRC levels are not significantly affected by CBLC, and CBLC knockdown does not phenocopy SRC activation, suggesting that CBLC's action at the Golgi is not direct downregulation of SRC. Altogether, our results demonstrate a role of CBLC in regulating Golgi ribbon by antagonizing the SRC tyrosine kinase. © 2015 Lee et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/165762
ISSN: 19326203
DOI: 10.1371/journal.pone.0138789
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