Recognition of misfolded glycoproteins in the endoplasmic reticulum / David Y. Thomas.

Format:

Video

Author/Creator:

Thomas, David Y., author.

Language:

English

Subjects (All):

Endoplasmic reticulum.

Physical Description:

1 online resource (1 streaming video file (57 min.)) : color, sound

Place of Publication:

London : Henry Stewart Talks Ltd, 2012.

System Details:

video file

Contents:

Introduction

Objectives

Role of quality control in cell processes

Eukaryotic cells are highly compartmentalized

The ER environment

ER protein folding and quality control

Protein folding: ribonuclease A

Molecular chaperones

Protein disulfide isomerase (PDI)

PDIs which are present in the lumen

Prolyl cis-trans isomerase (PPI)

Molecular chaperones and foldases in the ER

N-glycosylation

N-glycan precursor synthesis

Glc3Man9GlcNAc2 glycan trimming in the ER

Calnexin: a lectin type chaperone

Calnexin transiently interacts with glycoproteins

The calnexin cycle (1)

Calnexin binds monoglucosylated glycoproteins

Binding of Glc1Man9 RNaseB intermediates

Calnexin lumenal domain

The calnexin cycle (2)

ERp57

RNase B refolding, catalyzed by ERp57 or PDI (1)

RNase B refolding, catalyzed by ERp57 or PDI (2)

Mapping the ERp57 binding site on calnexin

ERp57 structure and the calnexin binding site

PPIs also interact with calnexin/calreticulin

PDI-bb' domains can bind hydrophobic peptides

UDP-glucose glucosyl glycoprotein transferase

Man9GlcNAc2 glycoproteins from yeast DT111

Glucosylation of Man9GlcNAc2 glycopeptides

Rank order of peptides glucosylated by UGGT

Structure of beta-glucanase

UGGT substrates can be mutant but active

The calnexin cycle (3)

Disposal of misfolded glycoproteins by ERAD

The fate of glycoproteins

The ER quality control apparatus

ER quality control

Concluding words.

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 13, 2024, from https://hstalks.com/bs/2224/.