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Proteostasis and protein secretion

Life and Matter Sciences International Symposium Thursday and Friday, October 17 and 18, 2019 9:15 hours Madrid

General information:

Venue: Fundación Ramón Areces. Calle Vitruvio, 5. 28006. Madrid.

Free admission. Necessary previous online registration. Limited capacity.

Coordinator:

Vivek Malhotra

Deputy coordinator:

Arkaitz Carracedo

Organized by:

Fundación Ramón Areces

In cooperation with:

Sociedad Española de Bioquímica y Biología Molecular (SEBBM)

Multimedia

Mariora Chiritoiu's full lecture

Multimedia

Pedro Carvalho's full lecture

Multimedia

Verónica Torrano's full lecture

Multimedia

Ishier Raote's full lecture

Multimedia

Fernando Martín Belmonte's full lecture

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Description
Programme

Producing the right quantities of proteins for their function within and outside the cells is of fundamental importance. These two processes controls cell compartmentation and its effects on the neighboring cells. Secretory proteins come in two forms: class one, which contain a signal sequence for entering the ER-Golgi pathway of protein secretion, and class two that is composed of proteins that lack a signal sequence and are therefore secreted without entering the ER, a process that we have termed “unconventional secretion.”

Class one proteins include insulin, antibodies, neurotransmitters and growth hormones. Examples of class II secretory proteins include interleukin1, FGF1 and FGF2, Diazepam binding inhibitor (also called Acb1), SOD1, and Galectin 3. Almost four decades ago, George Palade elucidated a route by which secretory proteins, after their synthesis in the endoplasmic reticulum (ER), are released by eukaryotic cells to the extracellular space. In the last four decades, the use of genetics and biochemical approaches have led to a detailed understanding of how secretory proteins are sorted, packed into specific transport carriers and delivered to their respective destinations within the cell and/or released in the extracellular space.

The last four decades have also revealed the existence of a system that controls how cells produce right quantities of proteins based on the cellular needs and how unwanted or excess of the products are cleared by degradation. Together, proteostasis and secretion are tightly linked and new findings are revealing the mechanism by which these two processes communicate to ensure the cells produce and secrete the right amounts of proteins. This meeting brings together experts to present their new findings and future directions to help us understand normal human physiology and to manipulate pathologies linked to dysregulated proteostasis and secretion.

Thursday, October 17

8:45 h.

Attendee check-in

9:15 h.

Welcome

Federico Mayor Zaragoza
Chair Scientific Council Fundación Ramón Areces.

Vivek Malhotra
Chair, Cell and Developmental Biology, Centre for Genomic Regulation (CRG).

9:30 h.

Keynote 1: Protein Folding Homeostasis in the Endoplasmic Reticulum

David Ron
Professor of Cellular Pathophysiology and Clinical Biochemistry, University of Cambridge. Fellow of The Royal Society. UK

Session 1: Stress, degradation and secretion

10:30 h.

GRASP55 and UPR Control Interleukin-1β Aggregation and Secretion

Mariora Chiritoiu
Group leader, Institute of Biochemistry of the Romanian Academy, Bucharest, Romania.

11:15 h.

Mechanisms of organelle biogenesis and quality control

Pedro Carvalho
Professor, Sir William Dunn School of Pathology, Oxford, UK.

12:00 h.

Break

12:15 h.

Regulation of secretion in the early secretory pathway by stress

Catherine Rabouille
Professor Hubrecht University for Developmental Biology and Stem Cell Research, Utrecht, Netherland.

13:00 h.

Break

Session 2: Cytoplasmic degradation

15:45 h.

Exploration of SUMO and other ubiquitin-like proteins in proteostasis

Rosa Barrio
Investigadora Principal del grupo de "Desarrollo y procesos relacionados con ubiquitinación", CIC bioGUNE, Center for Cooperative Research in Biosciences, Spain.

16:30 h.