Increased Polyubiquitination and Proteasomal Degradation of a Munc18-1 Disease-Linked Mutant Causes Temperature-Sensitive Defect in Exocytosis
Summary: Munc18-1 is a critical component of the core machinery controlling neuroexocytosis. Recently, mutations in Munc18-1 leading to the development of early infantile epileptic encephalopathy have been discovered. However, which degradative pathway controls Munc18-1 levels and how it impacts on...
Main Authors: | Sally Martin, Andreas Papadopulos, Vanesa M. Tomatis, Emma Sierecki, Nancy T. Malintan, Rachel S. Gormal, Nichole Giles, Wayne A. Johnston, Kirill Alexandrov, Yann Gambin, Brett M. Collins, Frederic A. Meunier |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2014-10-01
|
Series: | Cell Reports |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124714007359 |
Similar Items
-
Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis
by: Lu Ma, et al.
Published: (2015-12-01) -
Molecular mechanisms of polyubiquitin recognition by the proteasome and ubiquitin-associated domains
by: Trempe, Jean-François
Published: (2006) -
Role of Munc13 Isoforms in Regulating Large Dense Core Vesicle Exocytosis in Chromaffin Cells
by: Man, Kwun Nok Mimi
Published: (2015) -
Identification of a Munc13-sensitive step in chromaffin cell large dense-core vesicle exocytosis
by: Kwun Nok M Man, et al.
Published: (2015-11-01) -
Large Dense Core Vesicle Exocytosis in Mouse Chromaffin Cells is Regulated by Munc13s and Baiap3
by: Shin, Yong
Published: (2012)