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- W2202220006 abstract "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." @default.
- W2202220006 created "2016-06-24" @default.
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- W2202220006 creator A5068252474 @default.
- W2202220006 creator A5085355559 @default.
- W2202220006 creator A5088076447 @default.
- W2202220006 date "2016-01-01" @default.
- W2202220006 modified "2023-09-27" @default.
- W2202220006 title "Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking" @default.
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- W2202220006 doi "https://doi.org/10.1091/mbc.e15-09-0650" @default.
- W2202220006 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4694753" @default.
- W2202220006 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26538023" @default.
- W2202220006 hasPublicationYear "2016" @default.
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