PROTEIN MODIFICATION, TRAFFICKING AND DEGRADATION
Ubiqutin & Ubiqutin-like Modifications
The Multivesicular Body & Endocytosis
Mechanisms of Bacterial Pathogenesis
Regulatory Thiol Modifications
Proteomics of Post-translational Modifications (workshop
For more details, go to the ASBMB 2013 meeting program page
and click to expand “Protein Modification, Trafficking and Degradation.”
Although the central dogma of molecular biology is DNA → RNA → Protein, we can’t declare victory once the protein is made. A major focus of biological regulation is the chemical modification of amino acid side chains of proteins with molecules as large as a protein or as small as a methyl group. These myriad modifications enable rapid, flexible and finely tuned responses to changing conditions in the cell. The ability to follow these chemical modifications globally and quantitatively by mass spectrometry is having a marked impact on our understanding of biological regulation and human health. The “Protein Modification, Trafficking and Degradation” theme examines the mechanisms and consequences of protein modification in four sessions, which are complemented by a workshop at which experts will share the state of the art on the proteomics of post-translational modifications.
Marked for destruction or just a change of address
Misfolded proteins are toxic and have been implicated in tens of diseases. We will examine how the ubiquitin-proteasome pathway identifies such proteins, tags them covalently, and rids them from the cell. The elimination of membrane proteins also involves ubiquitination, although they are directed to the lysosome for elimination rather than the proteasome. The relevant trafficking pathways, endocytosis and the multivesicular body, form a novel and rapidly developing area of cell biology.
Host vs. pathogen
Bacteria usurp the eukaryotic cellular machinery to invade and sicken their hosts. We will learn how bacteria attempt hostile takeovers, how the host fights back and how the mycobacterial proteasome might represent a new target for treating tuberculosis.
An inviting site for chemistry, cysteine residues in proteins are modified in ways that control protein localization, sense changes in the environment and regulate enzyme activity. The versatility of cysteine modifications in proteins will be highlighted in a session that explores topics from a redox regulatory switch with implications for diabetes and obesity to oxygen sensing in plants.
Daniel Finley (email@example.com) is a professor at Harvard Medical School. Maurine E. Linder (firstname.lastname@example.org) is a professor at Cornell University.