Key result
Depletion of MYO1C induces Golgi apparatus fragmentation and decompaction, and delays the arrival of incoming transport carriers from both anterograde and retrograde routes.
MYO1C is a novel regulator at the Golgi apparatus that stabilizes branched actin to facilitate the arrival of incoming transport carriers.
MYO1C depletion disrupts Golgi integrity in animal cells; leaves open its role in human cardiovascular trafficking and disease.
We aim at the identification of myosin motor proteins that control trafficking at the Golgi apparatus. In addition to the known Golgi-associated myosins MYO6, MYO18A and MYH9 (myosin IIA), we identify MYO1C as a novel player at the Golgi. We demonstrate that depletion of MYO1C induces Golgi apparatus fragmentation and decompaction. MYO1C accumulates at dynamic structures around the Golgi apparatus that colocalize with Golgi-associated actin dots. Interestingly, MYO1C depletion leads to loss of cellular F-actin, and Golgi apparatus decompaction is also observed after the inhibition or loss of the Arp2/3 complex. We show that the functional consequences of MYO1C depletion is a delay in the arrival of incoming transport carriers, both from the anterograde and retrograde routes. We propose that MYO1C stabilizes branched actin at the Golgi apparatus that facilitates the arrival of incoming transport at the Golgi.
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Capmany et al. (2018) studied Golgi apparatus trafficking (In vitro). MYO1C depletion via siRNA vs. Control siRNA (Luciferase) was evaluated on Golgi apparatus morphology and arrival of incoming transport carriers. Depletion of MYO1C induces Golgi apparatus fragmentation and decompaction, and delays the arrival of incoming transport carriers from both anterograde and retrograde routes.
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