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Lecture

Glycosylation-Folding and Quality Control

In course

BIO-207: Cellular and molecular biology II

This course is aimed to familiarize students with the 3D organization of a eukaryotic cell, its compartmentalization, how cellular compartments communicate together and how a cell communicates with its environment. The related molecular mechanisms will be ...

Description

This lecture covers proteolytic cleavage, isomerization of prolines, post-translational modifications, protein folding influenced by GPI anchoring, disulfide bond formation, chaperones' role in protein folding, folding defects causing genetic diseases like Hyaline Fibromatosis Syndrome, N- and O-linked glycosylation, and quality control mechanisms in protein synthesis.

Instructors (3)

Françoise Gisou van der Goot Grunberg

Gisou van der Goot is the Head of the Laboratory of Cell and Membrane Biology, and founding member of the Global Health Institute (GHI), School of Life Sciences, at the Swiss Federal Institute of Technology Lausanne/EPFL (Ecole Polytechnique Fédérale de Lausanne). She is currently Vice President for Responsible Transformation, in charge of reinforcing values such as inclusion and sustainability throughout the School’s campus. From 2014 to 2020, she was Dean of the School of Life Sciences. Before joining EPFL, she was Group Leader at the Faculty of Sciences of the University of Geneva (UNIGE) and subsequently Associate Professor at the Faculty of Medicine of the same university. She studied engineering at the Ecole Centrale de Paris, then did a PhD in Molecular Biophysics at the Nuclear Energy Research Center, Saclay, France, followed by a postdoc at the European Molecular Biology Laboratory (EMBL) in Heidelberg. She obtained an EMBO Young Investigator award in 2001, a Howard Hughes International Scholar award in 2005 and the Swiss Prix Marcel Benoist in 2009, the same year she was elected EMBO member (European Molecular Biology Organisation). She is a leader in the fields of molecular and cellular understanding of bacterial toxins, the organization of mammalian membranes and in organelles biology. Professor van der Goot is member of diverse scientific boards such as the Swiss National Science Foundation (SNF), the Conseil suisse de la science et de la technologie (CSST) and the European Research Council (ERC).

Wouter Richard Karthaus

Romain Zufferey

Official source

Related concepts (32)

Glycosylation

Glycosylation is the reaction in which a carbohydrate (or 'glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. Glycosylation is a form of co-translational and post-translational modification.

O-linked glycosylation

O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity.

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.

Quality control

Quality control (QC) is a process by which entities review the quality of all factors involved in production. ISO 9000 defines quality control as "a part of quality management focused on fulfilling quality requirements". This approach places emphasis on three aspects (enshrined in standards such as ISO 9001): Elements such as controls, job management, defined and well managed processes, performance and integrity criteria, and identification of records Competence, such as knowledge, skills, experience, and qualifications Soft elements, such as personnel, integrity, confidence, organizational culture, motivation, team spirit, and quality relationships.

Glycoprotein

Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions.

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