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Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking
- Source :
- Molecular Biology of the Cell
- Publication Year :
- 2016
- Publisher :
- American Society for Cell Biology (ASCB), 2016.
-
Abstract
- GRASP65 plays a role in Golgi ribbon formation. Because the gaps between Golgi stacks are heterogeneous and large, it is possible that other proteins may help GRASP65 in ribbon linking. Mena is a novel GRASP65-binding protein that promotes actin elongation and enhances GRASP65 oligomerization to link Golgi stacks into a ribbon.<br />In mammalian cells, the Golgi reassembly stacking protein 65 (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers through the N-terminal GRASP domain. Because the GRASP domain is globular and relatively small, but the gaps between stacks are large and heterogeneous, it remains puzzling how GRASP65 physically links Golgi stacks into a ribbon. To explore the possibility that other proteins may help GRASP65 in ribbon linking, we used biochemical methods and identified the actin elongation factor Mena as a novel GRASP65-binding protein. Mena is recruited onto the Golgi membranes through interaction with GRASP65. Depleting Mena or disrupting actin polymerization resulted in Golgi fragmentation. In cells, Mena and actin were required for Golgi ribbon formation after nocodazole washout; in vitro, Mena and microfilaments enhanced GRASP65 oligomerization and Golgi membrane fusion. Thus Mena interacts with GRASP65 to promote local actin polymerization, which facilitates Golgi ribbon linking.
- Subjects :
- 0301 basic medicine
Golgi ribbon formation
Golgi Apparatus
macromolecular substances
Golgi reassembly
Biology
Bioinformatics
Microfilament
Autoantigens
Membrane Fusion
Polymerization
03 medical and health sciences
chemistry.chemical_compound
symbols.namesake
Golgi membrane fusion
Humans
RNA, Small Interfering
Molecular Biology
Actin
fungi
Microfilament Proteins
Golgi Matrix Proteins
Membrane Proteins
Articles
Intracellular Membranes
Cell Biology
Microfilament Protein
Golgi apparatus
Actins
body regions
Nocodazole
030104 developmental biology
nervous system
chemistry
Membrane Trafficking
Biophysics
symbols
sense organs
HeLa Cells
Subjects
Details
- ISSN :
- 19394586 and 10591524
- Volume :
- 27
- Database :
- OpenAIRE
- Journal :
- Molecular Biology of the Cell
- Accession number :
- edsair.doi.dedup.....92cbc37e711d56d587c16d540f743f33