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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Protein Trafficking In The Endoplasmic Reticulum Mediated By A Tpr-Containing Adapter Protein, Nathan P. Canniff
Protein Trafficking In The Endoplasmic Reticulum Mediated By A Tpr-Containing Adapter Protein, Nathan P. Canniff
Doctoral Dissertations
The endoplasmic reticulum (ER) is a large, multifunctional organelle that acts as the entrance into the secretory pathway, which accounts for the folding and maturation of approximately one third of the human proteome. It is the largest organelle in most cell types and is comprised of a single lumen and a contiguous membrane. The ER is responsible for a multitude of roles including protein translocation, folding, maturation, quality control, and glycosylation to name a few. These processes are buoyed by a large collection of chaperones and cochaperones, the largest subfamily of which is characterized by the presence of tetratricopeptide repeat …
Tpr-Containing Proteins Control Protein Organization And Homeostasis For The Endoplasmic Reticulum, Jill Bradley-Graham
Tpr-Containing Proteins Control Protein Organization And Homeostasis For The Endoplasmic Reticulum, Jill Bradley-Graham
Doctoral Dissertations
The endoplasmic reticulum (ER) is a complex, multifunctional organelle comprised of a continuous membrane and lumen that is organized into several functional regions. It plays various roles including protein translocation, folding, quality control, secretion, calcium signaling, and lipid biogenesis. Cellular protein homeostasis is maintained by a complicated chaperone network, and the largest functional family within this network consists of proteins containing tetratricopeptide repeats (TPRs). TPRs are well-studied structural motifs that mediate intermolecular protein-protein interactions, supporting interactions with a wide range of ligands or substrates. Nine TPR-containing proteins have been shown to localize to the ER and control protein organization and …
New Insights Into The Role Of The Udp-Glucose: Glycoprotein Glucosyltransferase 1 In The Endoplasmic Reticulum Quality Control, Abla Tannous
New Insights Into The Role Of The Udp-Glucose: Glycoprotein Glucosyltransferase 1 In The Endoplasmic Reticulum Quality Control, Abla Tannous
Doctoral Dissertations
The UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1) is a central quality control factor in the Endoplasmic Reticulum (ER). It surveys the folding status of proteins in the ER and redirects them, via its reglucosylation activity, to bind to the ER carbohydrate binding (lectin) chaperones calreticulin (CRT) and calnexin (CNX). However, the cellular mechanism of UGT1 is not completely understood. Using a cell based reglucosylation assay, we found that UGT1 reglucosylated proteins that eventually fold. This modification was transient and resulted in delay of protein trafficking in the secretory pathway and prolonged binding to lectin chaperones in the ER. In addition, terminally misfolded …