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SUMMARY:Ubiquitin - How a small protein regulates complex signalling casca
 des - Kirstin Keusekotten
DTSTART:20130314T131000Z
DTEND:20130314T140000Z
UID:TALK42270@talks.cam.ac.uk
CONTACT:Sven Friedemann
DESCRIPTION:Cells and tissues in our body are challenged every day with ne
 w environmental situations. For example\, sunburn damages your DNA in the 
 respective skin cells and bacteria or viruses try to exploit your body to 
 replicate themselves. Cells have evolved multiple specialised ways to sens
 e these stresses and form it into a signal in order to avoid further damag
 e and alert surrounding cells.\nThey do so through complex signalling casc
 ades\, whose components are present within all cells and are only activate
 d upon stimulation to stress. This activation is mediated and amplified mo
 stly by protein modifications such as the attachment of a small chemical g
 roup (e.g. a phosphate) and/or the attachment of small proteins.\nThe most
  prominent and most versatile member of protein attachment is ubiquitin. W
 e are only just beginning to appreciate the subtlety of this modification 
 since ubiquitin can itself be modified by another ubiquitin molecule on ei
 ght different attachment points. This results in the formation of ubiquiti
 n chains of different linkage types\, all of which\, form different signal
 s being generated\, read and disassembled by specialised proteins. Compare
 d to the rather simple binary code used in IT or even the 4-letter code us
 ed in DNA\, the ubiquitin code seems therefore to be much more complex. Th
 e talk will highlight this complexity by explaining the roles of ubiquitin
  within the inflammatory TNF/NFB pathway\, thereby including our latest
  finding of a new NFB regulator that disassembles only one chain type.\
 n
LOCATION:1 Newnham Terrace\, Darwin College
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