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SUMMARY:Structural and Biochemical Analysis of Full-Length Huntingtin Illu
 minate the Impact of the Polyglutamine Region
DTSTART:20170609T150000
DTSTAMP:20260510T082000Z
UID:f70aad18fa9e40ba15fb951aa5565530815d68e457ebe7a865c4f39c
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Ji-Joon Song\, KAIST\, Daejeon (KOR)\nBIOENGINEERING SEM
 INAR\n\nAbstract:\nThe polyglutamine expansion in huntingtin protein cause
 s Huntington’s disease but it remains unclear how this mutation alters f
 ull-length huntingtin structure and function. Here\, we investigated the e
 ffects of the polyglutamine tract expansion on bio-physicochemical propert
 ies of huntingtin. We analyzed the 3D structures and the intra-molecular i
 nteractions of Q23- and Q78-huntingtin by negatively-stained electron micr
 oscopy and cross-linking mass spectrometry respectively\, indicating that 
 huntingtin adopts a spherical shape with a large central cavity and folds 
 back to enable many intra-molecular interactions. Using a panel of highly 
 purified human recombinant huntingtins with polyglutamine lengths of 2\, 2
 3\, 46\, 67 and 78 residues\, we found that the polyglutamine expansion ap
 parently increases the α-helicity of huntingtin\, and alters huntingtin p
 hosphorylation sites to modulate huntingtin’s function of stimulating PR
 C2 histone methyltransferase activity. Our works provide the first glimpse
  into the structure of full-length huntingtin and reveal the effect of pol
 yglutamine expansion on full-length huntingtin phosphorylation and functio
 n.\n\nBio:\n2009–2013 Assistant Professor\nDepartment of Biological Scie
 nces\nKAIST\, Daejeon\, South Korea\n\n2005–2009 Postdoctoral Research F
 ellow\, Jane Coffin Childs Fellow\nDepartment of Molecular Biology and Gen
 etics\nMassachusetts General Hospital\, Harvard Medical School\, MA\, USA.
 \n\n2001–2005 Doctoral Student\nWatson School of Biological Sciences\nCo
 ld Spring Harbor Laboratory\, NY\, USA
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
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