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Moreover, ER stress rapidly reduces the transport to the Golgi complex of the temperature sensitive mutant of the Vesicular Stomatitis Virus G Glycoprotein (VSV-G) fused with the Green Fluorescent Protein (ts045G), without apparently decreasing the amount of the protein competent for export.
A vital aspect to efficient export of proteins from the ER is to ensure that only those proteins that are correctly folded and assembled are competent for export.
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Phosphorylation of Siz1p during mitosis renders the protein competent for nuclear export by Msn5p/Kap142p and, as a result, Siz1p relocalizes to the cytoplasm where it mediates septin sumoylation (Makhnevych et al. 2007).
Proteins that transit the Tat pathway do so because they fold too rapidly to remain competent for Sec-dependent export [18] or because they bind protein subunits [9], [19] and/or redox cofactors [20], such as FeS clusters or molybdopterin centers, in the cytoplasm.
In turn the ADP-bound form of GRP78 binds the protein substrates and holds them in a dislocation-competent state until they are transferred to the retrotranslocation channel in the ER membrane, for export to the cytosol and subsequent ubiquitination and degradation.
Lobsters are caught for export.
At home, they make things for export.
Some coffee is grown for export.
The gas is liquefied for export.
Copra and seaweed are produced for export.
Evaporation works produce salt for export.
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