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TitleThe Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain.
Journal, issue, pagesStructure, Vol. 28, Issue 9, Page 1035-11050.e8, Year 2020
Publish dateSep 1, 2020
AuthorsTaeyang Jung / Baehyun Shin / Giorgio Tamo / Hyeongju Kim / Ravi Vijayvargia / Alexander Leitner / Maria J Marcaida / Juan Astorga-Wells / Roy Jung / Ruedi Aebersold / Matteo Dal Peraro / Hans Hebert / Ihn Sik Seong / Ji-Joon Song /
PubMed AbstractThe polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural ...The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural information on its HEAT-repeat domains. Here, we present analyses of the impact of polyQ length on the structure and function of HTT via an integrative structural and biochemical approach. The cryo-EM analysis of normal (Q23) and disease (Q78) type HTTs shows that the structures of apo HTTs significantly differ from the structure of HTT in a HAP40 complex and that the polyQ expansion induces global structural changes in the relative movements among the HTT domains. In addition, we show that the polyQ expansion alters the phosphorylation pattern across HTT and that Ser2116 phosphorylation in turn affects the global structure and function of HTT. These results provide a molecular basis for the effect of the polyQ segment on HTT structure and activity, which may be important for HTT pathology.
External linksStructure / PubMed:32668197
MethodsEM (single particle)
Resolution9.6 - 18.2 Å
Structure data

10793

6yej

EMDB-10793, PDB-6yej:
Cryo-EM structure of the Full-length disease type human Huntingtin
Method: EM (single particle) / Resolution: 18.2 Å

4937

6rmh

EMDB-4937: Cryo-EM 3D map of normal Huntingtin
PDB-6rmh: The Rigid-body refined model of the normal Huntingtin.
Method: EM (single particle) / Resolution: 9.6 Å

EMDB-4944:
Cryo-EM 3D map of the N-terminal GFP tagged normal type Huntingtin
Method: EM (single particle) / Resolution: 15.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / multivalent scaffold platform / STRUCTURAL PROTEIN

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