Green light for Golgi traffic

Article Abstract:

Eukaryotic cells secrete proteins by a ciruitous route, folding and assembling within the endoplasmic reticulum (ER), transported to the Golgi apparatus. It has been widely accepted that the process involves the budding and fusion of small vesicles, and Presley and colleagues have shown that proteins emerge at random sites over a cell, with the use of green fluorescent protein (GFP). The sites are marked by groups of vesicles and tubules (VTCs) which have undergone extensive electron microscopy studies.

Usage, Eukaryotic cells, Cells (Biology), Eukaryotes, Fluorescence microscopy

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A SNARE-like protein required for traffic through the Golgi complex

Article Abstract:

The yeast membrane protein, Sft1p, contains a large amount of phenylalanine and its structure is similar to that of the v-soluble NSF attachment protein receptor (SNARE) protein. SFT1 gene is necessary for normal growth and the abnormal growth of the sft-1 mutants can be removed by overexpression of SED5 which encodes the tSNARE, Sed5p, indicating a reciprocal interaction. Studies show that Sed5p is involved in endoplasmic reticulum-Golgi transport and in the intra-Golgi step which requires Stf1p.

Biological transport, Golgi apparatus

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Homotypic vacuolar fusion mediated by t- and v-SNAREs

Article Abstract:

Cell membrane research has established the integral membrane proteins v-SNAREs and t-SNAREs are located on the yeast vacuolar membrane. Vesicular v-SNAREs and target organelle t-SNAREs appear to compliment each other in the docking process. In vitro studies show that both types are needed before docking can occur. N-ethylmaleimide-sensitive fusion proteins (NSF/Sec18p) and soluble NSF attachment proteins (SNAPs/Sec17p) are involved during the priming stage of membrane fusion.

Membrane proteins, Membrane fusion, Cell organelles, Organelles

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