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Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1292310239

Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

About this item

Full title

Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

Publisher

United States: Public Library of Science

Journal title

PloS one, 2009-12, Vol.4 (12), p.e8372-e8372

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Ataxin-1 (Atx1), a member of the polyglutamine (polyQ) expanded protein family, is responsible for spinocerebellar ataxia type 1. Requirements for developing the disease are polyQ expansion, nuclear localization and phosphorylation of S776. Using a combination of bioinformatics, cell and structural biology approaches, we have identified a UHM ligan...

Alternative Titles

Full title

Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1292310239

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1292310239

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0008372

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