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The structural basis of Laminin:cell interactions

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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
Speaker:David Briggd
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  • In category "Seminar"
  • In group "(FLS) Special Seminars"
  • By Faculty of Life Sciences

"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."

Speaker

David Briggd

Organisation: Imperial College London

  • https://about.me/david_briggs

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Michael Smith Building
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Anna Fildes

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anna.fildes@manchester.ac.uk

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