scholarly journals The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release

2021 ◽  
Vol 41 (13) ◽  
pp. 2828-2841
Author(s):  
Hui-Ju Yang ◽  
Pin-Chun Chen ◽  
Chien-Ting Huang ◽  
Tzu-Lin Cheng ◽  
Sheng-Ping Hsu ◽  
...  
Genetics ◽  
2014 ◽  
Vol 196 (3) ◽  
pp. 601-604 ◽  
Author(s):  
Stephen Nurrish

2009 ◽  
Vol 186 (6) ◽  
pp. 897-914 ◽  
Author(s):  
Marija Sumakovic ◽  
Jan Hegermann ◽  
Ling Luo ◽  
Steven J. Husson ◽  
Katrin Schwarze ◽  
...  

Small guanosine triphosphatases of the Rab family regulate intracellular vesicular trafficking. Rab2 is highly expressed in the nervous system, yet its function in neurons is unknown. In Caenorhabditis elegans, unc-108/rab-2 mutants have been isolated based on their locomotory defects. We show that the locomotion defects of rab-2 mutants are not caused by defects in synaptic vesicle release but by defects in dense core vesicle (DCV) signaling. DCVs in rab-2 mutants are often enlarged and heterogeneous in size; however, their number and distribution are not affected. This implicates Rab2 in the biogenesis of DCVs at the Golgi complex. We demonstrate that Rab2 is required to prevent DCV cargo from inappropriately entering late endosomal compartments during DCV maturation. Finally, we show that RIC-19, the C. elegans orthologue of the human diabetes autoantigen ICA69, is also involved in DCV maturation and is recruited to Golgi membranes by activated RAB-2. Thus, we propose that RAB-2 and its effector RIC-19 are required for neuronal DCV maturation.


2012 ◽  
Vol 199 (6) ◽  
pp. 883-891 ◽  
Author(s):  
Rhea van de Bospoort ◽  
Margherita Farina ◽  
Sabine K. Schmitz ◽  
Arthur de Jong ◽  
Heidi de Wit ◽  
...  

Neuronal dense-core vesicles (DCVs) contain diverse cargo crucial for brain development and function, but the mechanisms that control their release are largely unknown. We quantified activity-dependent DCV release in hippocampal neurons at single vesicle resolution. DCVs fused preferentially at synaptic terminals. DCVs also fused at extrasynaptic sites but only after prolonged stimulation. In munc13-1/2–null mutant neurons, synaptic DCV release was reduced but not abolished, and synaptic preference was lost. The remaining fusion required prolonged stimulation, similar to extrasynaptic fusion in wild-type neurons. Conversely, Munc13-1 overexpression (M13OE) promoted extrasynaptic DCV release, also without prolonged stimulation. Thus, Munc13-1/2 facilitate DCV fusion but, unlike for synaptic vesicles, are not essential for DCV release, and M13OE is sufficient to produce efficient DCV release extrasynaptically.


Neuron ◽  
2001 ◽  
Vol 31 (3) ◽  
pp. 421-437 ◽  
Author(s):  
Robert Renden ◽  
Brent Berwin ◽  
Warren Davis ◽  
Kyoungsook Ann ◽  
Chin-Tang Chin ◽  
...  

2021 ◽  
Vol 2 (1) ◽  
pp. 100325
Author(s):  
Alessandro Moro ◽  
Rein I. Hoogstraaten ◽  
Claudia M. Persoon ◽  
Matthijs Verhage ◽  
Ruud F. Toonen

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