Proteomics

Dataset Information

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Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT


ABSTRACT: Identification of the binding interface between HttExon1Q48 and the molecular chaperone DNAJB1. The proteins were incubated and cross-linked in vitro and the binding interface was mapped to the hinge region between CTDI and CTDII of DNAJB1 and the proline rich domain of HTTEXon1Q48.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human) Escherichia Coli

SUBMITTER: Heike Stephanowitz  

LAB HEAD: Janine Kirstein

PROVIDER: PXD031214 | Pride | 2022-10-15

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
All_crosslinks_spectra_merged.pdf Pdf
DNAJB1-HTTQ48_XL.csv Csv
F1_20171023_HS785_2.raw Raw
F1_20180122_HS_HS819_JK_7_SDAmethod.raw Raw
HTTQ23-HSP70_XL.csv Csv
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Publications

Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT.

Ayala Mariscal S M SM   Pigazzini M L ML   Richter Y Y   Özel M M   Grothaus I L IL   Protze J J   Ziege K K   Kulke M M   ElBediwi M M   Vermaas J V JV   Colombi Ciacchi L L   Köppen S S   Liu F F   Kirstein J J  

Nature communications 20220810 1


Huntington's disease is a neurodegenerative disease caused by an expanded polyQ stretch within Huntingtin (HTT) that renders the protein aggregation-prone, ultimately resulting in the formation of amyloid fibrils. A trimeric chaperone complex composed of Hsc70, DNAJB1 and Apg2 can suppress and reverse the aggregation of HTTExon1Q<sub>48</sub>. DNAJB1 is the rate-limiting chaperone and we have here identified and characterized the binding interface between DNAJB1 and HTTExon1Q<sub>48</sub>. DNAJB  ...[more]

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