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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Song K,Gras C,Capin G,Gimber N,Lehmann M,Mohd S,Puchkov D,Rödiger M,Wilhelmi I,Daumke O,Schmoranzer J,Schürmann A,Krauss Mdoi
10.1242/jcs.225557subject
Has Abstractpub_date
2019-02-01 00:00:00issue
3eissn
0021-9533issn
1477-9137pii
132/3/jcs225557journal_volume
132pub_type
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