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Dysferlin Stimulates SNARE-mediated Membrane Fusion Molecular Biophysics
In this study we demonstrate a direct interaction between dysferlin and the SNARE proteins syntaxin 4 and SNAP-23. In addition, analysis of FRET and in vitro reconstituted lipid mixing assays indicate that dysferlin accelerates syntaxin 4/SNAP-23 heterodimer formation and SNARE-mediated lipid mixing in a calcium-sensitive manner. These results support a function for dysferlin as a calcium-sensing SNARE effector for membrane fusion events.
Source: Journal of Biological Chemistry - July 7, 2016 Category: Chemistry Authors: Codding, S. J., Marty, N., Abdullah, N., Johnson, C. P. Tags: Membrane Biology Source Type: research

Mutations Inhibits VCP SUMOylation and Stress Response Cell Biology
Valosin-containing protein/p97(VCP) is a hexameric ATPase vital to protein degradation during endoplasmic reticulum stress. It regulates diverse cellular functions including autophagy, chromatin remodeling, and DNA repair. In addition, mutations in VCP cause inclusion body myopathy, Paget disease of the bone, and frontotemporal dementia (IBMPFD), as well as amyotrophic lateral sclerosis. Nevertheless, how the VCP activities were regulated and how the pathogenic mutations affect the function of VCP during stress are not unclear. Here we show that the small ubiquitin-like modifier (SUMO)-ylation of VCP is a normal stress res...
Source: Journal of Biological Chemistry - June 30, 2016 Category: Chemistry Authors: Wang, T., Xu, W., Qin, M., Yang, Y., Bao, P., Shen, F., Zhang, Z., Xu, J. Tags: Molecular Bases of Disease Source Type: research