Lecture

Protein Phosphorylation: Mechanisms and Regulation

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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 provides an overview of post-translational modifications, focusing on phosphorylation. It covers the chemical modifications of amino acids, the most common types of phosphorylation, and the structural effects of phosphorylation in proteins. The lecture also discusses the importance of phosphorylation in signaling, enzyme regulation, and transcription factor activation. Furthermore, it delves into the activity and regulation of protein kinases, the human kinome, and the role of tyrosine phosphorylation. The lecture concludes with insights into kinase specificity, kinase pathways, and the implications of aberrant kinase activation in diseases like cancer.

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

Ontological neighbourhood

Biology

Cell biology: Cell signaling

Related concepts (32)

Mitogen-activated protein kinase

A mitogen-activated protein kinase (MAPK or MAP kinase) is a type of protein kinase that is specific to the amino acids serine and threonine (i.e., a serine/threonine-specific protein kinase). MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis.

Serine/threonine-specific protein kinase

A serine/threonine protein kinase () is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK). In enzymology, the term serine/threonine protein kinase describes a class of enzymes in the family of transferases, that transfer phosphates to the oxygen atom of a serine or threonine side chain in proteins.

Receptor tyrosine kinase

Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 58 encode receptor tyrosine kinase proteins. Receptor tyrosine kinases have been shown not only to be key regulators of normal cellular processes but also to have a critical role in the development and progression of many types of cancer.

Janus kinase

Janus kinase (JAK) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. They were initially named "just another kinase" 1 and 2 (since they were just two of many discoveries in a PCR-based screen of kinases), but were ultimately published as "Janus kinase". The name is taken from the two-faced Roman god of beginnings, endings and duality, Janus, because the JAKs possess two near-identical phosphate-transferring domains.

Tyrosine kinase

A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to the tyrosine residues of specific proteins inside a cell. It functions as an "on" or "off" switch in many cellular functions. Tyrosine kinases belong to a larger class of enzymes known as protein kinases which also attach phosphates to other amino acids such as serine and threonine. Phosphorylation of proteins by kinases is an important mechanism for communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division.

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