Mediaspace scheduled maintenance: Aug 25, 2026 07:00 - 12:00 AM. During this time, videos will be temporarily unavailable. Check status updates.

Lecture

BiP-mediated ER quality control: assists and hurdles

Description

This lecture explores the BiP-mediated ER quality control process, focusing on distinguishing nascent unfolded proteins from misfolded ones, targeting proteins for degradation, and assisting in proper folding. Unique challenges in B cell development are discussed, along with the role of chaperones in cellular and protein homeostasis.

Official source

Related concepts (32)

Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Homeostasis

In biology, homeostasis (British also homoeostasis) (/hɒmɪə(ʊ)ˈsteɪsɪs/) is the state of steady internal, physical, chemical, and social conditions maintained by living systems. This is the condition of optimal functioning for the organism and includes many variables, such as body temperature and fluid balance, being kept within certain pre-set limits (homeostatic range). Other variables include the pH of extracellular fluid, the concentrations of sodium, potassium, and calcium ions, as well as the blood sugar level, and these need to be regulated despite changes in the environment, diet, or level of activity.

Acid–base homeostasis

Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. The pH of the intracellular fluid and the extracellular fluid need to be maintained at a constant level. The three dimensional structures of many extracellular proteins, such as the plasma proteins and membrane proteins of the body's cells, are very sensitive to the extracellular pH.

Protein domain

In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions.

Related lectures (32)

Protein Folding: Mechanisms and Consequences

Explores protein folding, misfolding consequences, chaperones' role, and ATP importance.

Protein-Repair Machineries: Evolution and Function

Explores the evolution and function of protein-repair machineries, emphasizing the role of ATP-fueled unfolding machines in preventing protein aggregation and promoting proper folding.

Non-refoldability in E. coli Proteome

Delves into non-refoldability in the E. coli proteome, exploring protein folding challenges and implications.

Protein Folding Dynamics

Explores protein folding dynamics, chaperones, ATP hydrolysis, and DNA folding intricacies within the nucleus.

Post-translational regulation of ER proteostasis