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

Autor: Maria Rödiger, Dmytro Puchkov, Jan Schmoranzer, Gabrielle Capin, Oliver Daumke, Niclas Gimber, Ilka Wilhelmi, Martin Lehmann, Saif Mohd, Michael Krauss, Claudia Gras, Kyungyeun Song, Annette Schürmann
Rok vydání: 2019
Předmět:
Zdroj: Journal of Cell Science
ISSN: 1477-9137
0021-9533
DOI: 10.1242/jcs.225557
Popis: 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.
Highlighted Article: SEPT1 associates with the Golgi complex through GM130, and is required for maintaining Golgi architecture and function by connecting cis-Golgi membranes to the microtubule-nucleating machinery.
Databáze: OpenAIRE