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Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.

Journal of molecular biology - 23 Nov 2012

Mishra Rakesh, Hoop Cody L, Kodali Ravindra, Sahoo Bankanidhi, van der Wel Patrick C A, Wetzel Ronald

Abstract excerpt

Aggregation of expanded polyglutamine repeat-containing fragments of the huntingtin (htt) protein may play a key role in Huntington's disease. Consistent with this hypothesis, two Ser-to-Asp mutations in the 17-amino-acid N-terminal htt(NT) segment abrogate both visible brain aggregates and disease symptoms in a full-length Q(97) htt mouse model while compromising aggregation kinetics and aggregate morphology in...

Topics

Amino Acid Sequence
Amyloid
Animals
Exons
Humans
Huntingtin Protein
Kinetics
Mice
Molecular Sequence Data
Mutation
Nerve Tissue Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Serine

Thermodynamics

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Open in PubMed Open full text

Identifiers

PMID: 22999956
DOI: 10.1016/j.jmb.2012.09.011
PMCID: PMC3488119

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.PMID 22999956Read ↗

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Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.Semantic proximity Read ↗

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