Lecture

Protein Modifications: Ubiquitination and Acylation

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In course

BIO-212: Biological chemistry I

Biochemistry is a key discipline for the Life Sciences. Biological Chemistry I and II are two tightly interconnected courses that aim to describe and understand in molecular terms the processes that make life possible. ...

Description

This lecture covers the enzymatic mechanism of ubiquitin attachment to proteins, the role of ubiquitination in protein degradation, and the functions of ubiquitin-binding domains and deubiquitinases. It also explains the myristoylation and palmitoylation of proteins, the farnesylation and geranylgeranylation pathways, and the significance of Ras acylation for its cellular localization.

Instructors (4)

Matteo Dal Peraro

Matteo Dal Peraro graduated in Physics at the University of Padua in 2000. He obtained his Ph.D. in Biophysics at the International School for Advanced Studies (SISSA, Trieste) in 2004. He then received postdoctoral training at the University of Pennsylvania (Philadelphia) under the guidance of Prof. M. L. Klein. He was nominated Tenure Track Assistant Professor at the EPFL School of Life Sciences in late 2007. His research at the Laboratory for Biomolecular Modeling (LBM), within the Interfaculty Institute of Bioengineering (IBI), focuses on the multiscale modeling of large macromolecular systems.

Bruno Emanuel Ferreira De Sousa Correia

Throughout my PhD and postdoctoral studies I was trained in world-renowned laboratories and institutions in the United States of America (University of Washington and The Scripps Research Institute). Very early in my scientific career I found out my fascination about protein structure and function. My PhD studies evolved in the direction of immunogen design and vaccine engineering which sparked my interest in the many needs and opportunities in vaccinology and translational research. My efforts resulted in an enlightening piece of work where for the first time, computationally designed immunogens elicited potent neutralizing antibodies. During my postdoctoral studies I joined a chemical biology laboratory at the Scripps Research Institute. In this stage I developed novel chemoproteomics methods for the identification of protein-small molecule interaction sites in complex proteomes. In March 2015, I joined the École Polytechnique Fédérale de Lausanne (EPFL) – Switzerland as a tenure track assistant professor. The focus of my research group is to develop computational tools for protein design with particular emphasis in applying these strategies to immunoengineering (e.g. vaccine and cancer immunotherapy). The activities in my laboratory focus on computational design methods development and experimental characterization of the designed proteins. Our laboratory has been awarded with 2 prestigious research grants from the European Research Council. Lastly, I have been awarded the prize for best teacher of Life sciences in 2019.

Giovanni D'Angelo

Teaching & PhD PhD Students Mélissa Ruiz, Gary Domeniconi, Irmak Kaysudu, Alessandro Valente, Surayyo Akramkhanova, Jean Andrea Maillat, Linda Wedemann, Manel Leila Nadia Boussouf, Jiayan Lin, Nika Gorsek, Christina Ulrich, William Daniel Chan-Ha Verdier Past EPFL PhD Students Laura Capolupo, Jaipreet Singh Loomba, Halima Hannah Emilie Schede Past EPFL PhD Students as codirector Muhammad Umair Anwar Courses Biological chemistry II BIO-213 Biochemistry is a key discipline in the Life Scienc

Official source

Related concepts (32)

Proteasome

Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases. Proteasomes are part of a major mechanism by which cells regulate the concentration of particular proteins and degrade misfolded proteins. Proteins are tagged for degradation with a small protein called ubiquitin. The tagging reaction is catalyzed by enzymes called ubiquitin ligases.

Ubiquitin-conjugating enzyme

Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein.

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 targeting

Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, the plasma membrane, or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell; errors or dysfunction in sorting have been linked to multiple diseases.

G protein

G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are 'on', and, when they are bound to GDP, they are 'off'. G proteins belong to the larger group of enzymes called GTPases.

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