Regulation of ataxin-1 phosphorylation and its impact on biology

Sarita Lagalwar; Harry T. Orr

doi:10.1007/978-1-62703-411-1_13

Regulation of ataxin-1 phosphorylation and its impact on biology

Sarita Lagalwar, Harry T. Orr

Laboratory Medicine and Pathology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

9 Scopus citations

Abstract

Ataxin-1 protein expression is found in the cytoplasm and nucleus of Purkinje cells, the primary site of spinocerebellar ataxia type 1 (SCA1). Phosphorylation at S776 occurs in the cytoplasm and stabilizes the protein through interaction with 14-3-3, allowing it to translocate into the nucleus where disease is initiated. Phosphorylation and stabilization are enhanced when the polyglutamine expansion is present. In this chapter, we present a model of neurodegeneration in SCA1 initiated through phosphorylation at S776 by cAMP-dependent protein kinase (PKA) and enhanced by the presence of the polyglutamine expansion. The biological methods used to uncover SCA1 pathogenesis and phosphorylation at S776 are described.

Original language	English (US)
Title of host publication	Trinucleotide Repeat Protocols
Publisher	Humana Press Inc.
Pages	201-209
Number of pages	9
ISBN (Print)	9781627034104
DOIs	https://doi.org/10.1007/978-1-62703-411-1_13
State	Published - 2013

Publication series

Name	Methods in Molecular Biology
Volume	1010
ISSN (Print)	1064-3745

Keywords

14-3-3
Ataxin-1
Dephosphorylation
PKA
PP2A
Phosphorylation
Polyglutamine expansion
RBM-17
SCA1
U2AF65

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10.1007/978-1-62703-411-1_13

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title = "Regulation of ataxin-1 phosphorylation and its impact on biology",

abstract = "Ataxin-1 protein expression is found in the cytoplasm and nucleus of Purkinje cells, the primary site of spinocerebellar ataxia type 1 (SCA1). Phosphorylation at S776 occurs in the cytoplasm and stabilizes the protein through interaction with 14-3-3, allowing it to translocate into the nucleus where disease is initiated. Phosphorylation and stabilization are enhanced when the polyglutamine expansion is present. In this chapter, we present a model of neurodegeneration in SCA1 initiated through phosphorylation at S776 by cAMP-dependent protein kinase (PKA) and enhanced by the presence of the polyglutamine expansion. The biological methods used to uncover SCA1 pathogenesis and phosphorylation at S776 are described.",

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AU - Orr, Harry T.

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AB - Ataxin-1 protein expression is found in the cytoplasm and nucleus of Purkinje cells, the primary site of spinocerebellar ataxia type 1 (SCA1). Phosphorylation at S776 occurs in the cytoplasm and stabilizes the protein through interaction with 14-3-3, allowing it to translocate into the nucleus where disease is initiated. Phosphorylation and stabilization are enhanced when the polyglutamine expansion is present. In this chapter, we present a model of neurodegeneration in SCA1 initiated through phosphorylation at S776 by cAMP-dependent protein kinase (PKA) and enhanced by the presence of the polyglutamine expansion. The biological methods used to uncover SCA1 pathogenesis and phosphorylation at S776 are described.

KW - 14-3-3

KW - Ataxin-1

KW - Dephosphorylation

KW - PKA

KW - PP2A

KW - Phosphorylation

KW - Polyglutamine expansion

KW - RBM-17

KW - SCA1

KW - U2AF65

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BT - Trinucleotide Repeat Protocols

PB - Humana Press Inc.

ER -

Regulation of ataxin-1 phosphorylation and its impact on biology

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