The structural basis of Laminin:cell interactions
|Dates:||26 May 2016|
|Times:||13:00 - 14:00|
|What is it:||Seminar|
|Organiser:||Faculty of Life Sciences|
|Who is it for:||University staff, Current University students|
"Laminins are large heterotrimeric extracellular matrix proteins essential for correct formation of basement membranes. Binding of the c-termini of laminins to cells occurs via two mechanisms; either integrin- or dystroglycan-mediated. Loss of dystroglycan-mediated laminin-binding results in aberrant formation of basement membranes. This leads to particularly severe forms of muscular dystrophy, called dystroglycanopathies (including Walker-Warburg syndrome) and other pathologies such as kidney diseases (such as FSGS and MCD) and various retinal abnormalities.
The binding motif within dystroglycan is a unique GAG-like polysaccharide called the “LARGE glycan”. The dystroglycan appears to be a novel class of receptor-proteoglycan, with an entirely novel synthesis pathway.
I will give a brief overview of laminin structure and function and review what is known about the novel dystroglycan modification. I will then go on to discuss our recent structural results concerning the molecular mechanisms of dystroglycan-mediated laminin adhesion."
Organisation: Imperial College London
Travel and Contact Information
Michael Smith Building