A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane

Article Abstract:

The analysis of the initial stages of cotranslational transport of the secretory protein preprolactin through mammalian endoplasmic reticulum (ER) reveals that a translocation substrate undergoes two identification processes before being permitted to go through the ER. After the identification of the signal sequence of the nascent polypeptide chain in the cytosol by the SRP, the chain is shifted to the membrane where a second signal identification step occurs for which the presence in the lipid bilayer of the Sec61p complex is necessary and adequate.

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TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation in to the endoplasmic reticulum

Article Abstract:

Research was conducted to characterize the regulatory components of the translocon that affect translocational pausing in the endoplasmic reticulum. Constructs were truncated at Stu1 before transcription to produce mRNA utilized in translocation intermediates while reconstitutions from crude detergent extracts were determined by modifying previous study procedures. Results identified a prerequisite for the membrane glycoprotein translocating chain-associated membrane protein to regulate the translocational pausing of a secretory protein.

Cytosol

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Tripartite management of unfolded proteins in the endoplasmic reticulum

Article Abstract:

Research has been conducted on protein misfolding in endoplasmic reticulum. The molecular mechanisms of the induction and attenuation systems have been examined.

Japan, Statistical Data Included, Analysis, Eukaryotic cells, Cells (Biology), Eukaryotes, Cell research, Cytological research

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