[BIC-announce] FW: TODAY - Special Seminar - April 18 - 2:00 pm - "Exploring the molecular basis of degenerative disorders using functional proteomics"

[Jennifer Chew, Ms.]

PLEASE DISCARD IF THIS IS A DUPLICATE.  Jennifer

From: MNISTAFF - Montreal Neurological Institute Staff [mailto:MNISTAFF at LISTS.MCGILL.CA] On Behalf Of Enza Ferracane, Ms.
Sent: Thursday, April 18, 2013 8:10 AM
To: MNISTAFF at LISTS.MCGILL.CA
Subject: TODAY - Special Seminar - April 18 - 2:00 pm - "Exploring the molecular basis of degenerative disorders using functional proteomics"


SPECIAL SEMINAR ANNOUNCEMENT:

Thursday, April 18 - 2pm

de Grandpré Communications Centre, MNI

"Exploring the molecular basis of degenerative disorders using functional proteomics"

Benoit Coulombe, PhD
Director, Gene Transcription and Proteomics Laboratory
Director, Proteomics Discovery Platform
Institut de recherches cliniques de Montréal (IRCM)

Dr. Coulombe's research focuses on decrypting and reprogramming the chaperone code to cure degenerative diseases.  He and his colleagues recently discovered that a novel family of methyltransferases preferentially targets molecular chaperones to regulate their activity (http://www.plosgenetics.org/article/info%3Adoi%2F10.1371%2Fjournal.pgen.1003210).

Summary

Methylation, or transfer of a single or multiple methyl groups (CH3), is one of many post-translational modifications that occur on proteins. Such modifications can, in turn, affect numerous aspects of a protein, notably cellular localization, turnover, activity, and molecular interactions. In addition to post-translational modifications, the structural organization of a protein or protein complex can also have a significant impact on its function and stability. A group of factors known as "molecular chaperones" aid newly synthesized proteins in reaching their native conformation or alternating between physiologically relevant states. We present here a new family of factors that promote methylation of chaperones and show that, at least in one case, this modification translates into a modulation in the activity of the substrate chaperone. Our results not only characterize the function of previously unknown gene products, uncover a new role for protein methylation as a regulatory pathway for chaperones, and define a novel regulatory mechanism for the chaperone VCP, whose deregulation is causative of neuromuscular diseases, but also suggest the existence of a post-translational modification code that regulates molecular chaperones. Further decrypting this "chaperone code" will help understanding how the functional organization of the proteome is orchestrated.




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