Journal article
The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal
Abstract
The first 17 amino acids of Huntington's disease (HD) protein, huntingtin, comprise an amphipathic alpha-helical domain that can target huntingtin to the endoplasmic reticulum (ER). N17 is phosphorylated at two serines, shown to be important for disease development in genetic mouse models, and shown to be modified by agents that reverse the disease phenotype in an HD mouse model. Here, we show that the hydrophobic face of N17 comprises a …
Authors
Maiuri T; Woloshansky T; Xia J; Truant R
Journal
Human Molecular Genetics, Vol. 22, No. 7, pp. 1383–1394
Publisher
Oxford University Press (OUP)
Publication Date
April 1, 2013
DOI
10.1093/hmg/dds554
ISSN
0964-6906
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Active Transport, Cell NucleusAmino Acid SequenceCell NucleusCiliaConsensus SequenceEndoplasmic Reticulum StressFatty Acids, UnsaturatedHEK293 CellsHumansHuntingtin ProteinHydrophobic and Hydrophilic InteractionsKaryopherinsMolecular Sequence DataNerve Tissue ProteinsNuclear Export SignalsPhosphorylationProtein Processing, Post-TranslationalProtein Structure, TertiaryReceptors, Cytoplasmic and Nuclearran GTP-Binding ProteinExportin 1 Protein