Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

A SEPT1-based scaffold is required for Golgi integrity and function

[thumbnail of Original Article]
Preview
PDF (Original Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
12MB
[thumbnail of Supplementary Information]
Preview
PDF (Supplementary Information) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
164MB

Item Type:Article
Title:A SEPT1-based scaffold is required for Golgi integrity and function
Creators Name:Song, K., Gras, C., Capin, G., Gimber, N., Lehmann, M., Mohd, S., Puchkov, D., Rödiger, M., Wilhelmi, I., Daumke, O., Schmoranzer, J., Schürmann, A. and Krauss, M.
Abstract:Compartmentalization of membrane transport and signaling processes is of pivotal importance to eukaryotic cell function. While plasma membrane compartmentalization and dynamics are well known to depend on the scaffolding function of septin GTPases, the roles of septins at intracellular membranes have remained largely elusive. Here, we show that the structural and functional integrity of the Golgi depends on its association with a septin 1 (SEPT1)-based scaffold, which promotes local microtubule nucleation and positioning of the Golgi. SEPT1 function depends on the Golgi matrix protein GM130 (also known as GOLGA2) and on centrosomal proteins, including CEP170 and components of γ-tubulin ring complex (γ-Turc), to facilitate the perinuclear concentration of Golgi membranes. Accordingly, SEPT1 depletion triggers a massive fragmentation of the Golgi ribbon, thereby compromising anterograde membrane traffic at the level of the Golgi.
Keywords:Septin, SEPT1, GM130, CEP170, Microtubule Nucleation, Golgi, Animals, Mice
Source:Journal of Cell Science
ISSN:0021-9533
Publisher:Company of Biologists
Volume:132
Number:3
Page Range:jcs225557
Date:1 February 2019
Official Publication:https://doi.org/10.1242/jcs.225557
PubMed:View item in PubMed

Repository Staff Only: item control page

Downloads

Downloads per month over past year

Open Access
MDC Library