A related article, "The history of cold fusion," reviews the early portion of this science controversy.
Regulated secretion in neurons and endocrine cells is mediated by a specialized version of SNARE-mediated membrane fusion (reviewed in [1]).
It is thought that complex formation between SNARE proteins from opposing membranes provide the energy that drives membrane fusion (reviewed in [ 1- 4], Fig. 1A & 1B).
The specific interactions of these complexes are necessary for the formation of the MVB and proper progression of endosomal lysosomal fusion (reviewed in [45]).
Rabs, a family of small GTPases, identify the formed vesicles and control their budding, uncoating, motility and fusion (reviewed by Markgraf et al., 2007; Stenmark, 2009).
SNAREs play a role in nearly all steps of autophagy, from the formation of the autophagosome, to its maturation and the autophagosome-lysosome fusion (reviewed in [ 37]).
The cleaved peptides undergo conformational changes, resulting in hairpin-like, alpha-helical bundles, which bring the viral and cell membranes into close apposition and thereby facilitates fusion (reviewed by Chen and Olson 2005).
It is thought that similar mechanisms mediate autophagosome lysosome and endosome lysosome fusion (reviewed in 29), so data presented here for a putative role for impaired Rab7 recruitment may also be of relevance to the reported deficits in autophagy.
Both C-myc and N-myc are highly expressed in RMS, with the highest expression observed in ARMS where N-myc is a transcriptional target of the PAX3-FOXO1 fusion (reviewed in Marshall and Grosveld (2012)).
The coat minimally consists of the small GTPase Arf1 and the heptameric coatomer complex (α-, β′-,β′-, γ-, δ-, ε-, and ζ-COP) and disassembles after vesicle formation in preparation for membrane fusion (reviewed in Duden 2003).
