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Lecture

Protein Synthesis and Addressing to the Nucleus

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 the rapid succession of protein synthesis and folding, the addressing of proteins to different compartments within the endomembrane system, and the Nobel Prize-winning discovery of protein addressing signals. It also explains the signal sequences for addressing proteins to various organelles, the nuclear pore complex structure, and the recognition of nuclear localization signals by nuclear transport receptors.

Instructors (3)

Wouter Richard Karthaus

Romain Zufferey

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).

Official source

Related concepts (25)

Nuclear pore

A nuclear pore is a channel as part of the nuclear pore complex (NPC), a large protein complex found in the nuclear envelope in eukaryotic cells, enveloping the cell nucleus containing DNA, which facilitates the selective membrane transport of various molecules across the membrane. The nuclear pore complex predominantly consists of proteins known as nucleoporins, with each NPC comprising at least 456 individual protein molecules, and 34 distinct nucleoporin proteins.

Nuclear localization sequence

A nuclear localization signal or sequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. Typically, this signal consists of one or more short sequences of positively charged lysines or arginines exposed on the protein surface. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal (NES), which targets proteins out of the nucleus. These types of NLSs can be further classified as either monopartite or bipartite.

Nuclear envelope

The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus, which encloses the genetic material. The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. The space between the membranes is called the perinuclear space. It is usually about 10–50 nm wide. The outer nuclear membrane is continuous with the endoplasmic reticulum membrane.

Signal peptide

A signal peptide (sometimes referred to as signal sequence, targeting signal, localization signal, localization sequence, transit peptide, leader sequence or leader peptide) is a short peptide (usually 16-30 amino acids long) present at the N-terminus (or occasionally nonclassically at the C-terminus or internally) of most newly synthesized proteins that are destined toward the secretory pathway. These proteins include those that reside either inside certain organelles (the endoplasmic reticulum, Golgi or endosomes), secreted from the cell, or inserted into most cellular membranes.

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.

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Protein Synthesis: Translation Process

Explores the translation process of protein synthesis, covering nuclear structure, ribosomes, tRNA, and translation accuracy.

Protein Localization: Mechanisms and Pathways in Cells

Covers the mechanisms of protein localization in cells, focusing on synthesis, sorting, and transport pathways involving the endoplasmic reticulum and Golgi apparatus.

Proteins: Central Dogma and Translation

Explains protein synthesis, translation, and the central dogma of molecular biology.

Protein Addressing at the Endoplasmic Reticulum

Explores protein addressing at the ER, including signal recognition and translocation mechanisms.

Protein Folding: Mechanisms and Consequences