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

Lecture

Proteostasis Regulation: Chaperone Interactions and Post-Translational Modifications

Description

This lecture delves into the intricate world of proteostasis regulation, focusing on the interactions between chaperones and post-translational modifications (PTMs). The instructor explores how Hsp70, a key chaperone, interacts with various proteins in the cell, shedding light on the crucial role of chaperones in maintaining protein homeostasis. Through advanced techniques like XL-MS, the lecture uncovers the complex network of biologically-important PTM-associated interactions, providing insights into protein folding, misfolding, and aggregation. The study of Hsp70's binding to PTMs and its impact on client interactions opens new avenues for understanding protein quality control mechanisms and their relevance in health and disease.

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.

Protein aggregation

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

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.

Proteinopathy Mapping: Connecting Proteotoxicity to Intrinsic Functions

Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.

Non-refoldability in E. coli Proteome

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

Protein Folding Dynamics