Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence

Article Abstract:

The role of the BOS1 product (Bos1p) in the transport of vesicles from the endoplasmic reticulum (ER) to the Golgi apparatus was investigated. Previous studies have shown that Bos1p is localized in the ER membrane and co-purifies with carrier vesicles. The study protocol involved an assay which reconstitutes transport between the ER and the Golgi apparatus. Anti-Bos1p antibodies blocked transport after ER budding but before fusion with the Golgi membranes, while depletion of Bos1p ER led to transport-incompetent vesicles. The results suggest a key role for Bos1p in the fusion competence of ER to Golgi transport vesicles.

Analysis, Membrane proteins, Membrane fusion

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Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells

Article Abstract:

Immunoprecipitation assay and immunofluorescence microscopy were performed to study the protein interactions that regulate vesicle transport between the cellular organelles, endoplasmic reticulum (ER) and Golgi apparatus. The results revealed that there exists an oligomeric complex representing an intermediate in the ER-to-Golgi transfer reactions. The complex was found to consist of syntaxin 5, GOS-28, membrin, msec22b, rbet1, and two Sec22p-related proteins the interactions of which determine vesicle docking/fusion fidelity between the two organelles during transport.

Usage, Carrier proteins, Transport proteins, Fluorescence microscopy, Cloning, Amino acid sequence, Amino acid sequencing, Immunoassay, DNA sequencers

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The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer

Article Abstract:

In the early stages of protein insertion, the protein-conducting channels of the endoplasmic reticulum have been found to be open laterally towards the lipid bilayer. The amount of opening of the channel may depend on the hydrophobicity of the signal or signal anchor sequence. The hydrophobic area is in contact with the lipids, and the translocating portion which is lipophobic is linked with the proteins.

Proteins, Lipid membranes, Bilayer lipid membranes

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