Eukaryotic cells contain multiple membrane-bound compartments between which proteins and lipid molecules are continually shuttled via membrane-bound vesicular carriers. Despite the constant flux of proteins and lipid through these compartments their functional and composition integrity is maintained. While the molecular machinery involved in vesicle recognition and fusion can often be transport-step/fusion-event specific, one group of proteins & #x2014; the SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) play a common and central role in this process. Transport-step-specific combinations of SNARE proteins, localized to the vesicle and the target organelle, form complexes that facilitate the final step leading to the fusion of vesicles with their cognate target organelles. In general, the role of SNAREs appears to be conserved irrespective of their location of function in the cell, and much of what has been established for SNAREs in a particular trafficking pathway or organelle, is broadly applicable to SNAREs that function in the Golgi. Here we review Golgi SNAREs and the role they play in membrane and protein trafficking in the Golgi apparatus with, a particular emphasis on their functions in yeast and human cells.
KeywordsMembrane Fusion Snare Complex Snare Protein Golgi Membrane Conserve Oligomeric Golgi
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