Nucleolar localization of aprataxin is dependent on interaction with nucleolin and on active ribosomal DNA transcription (Q24293612)

protein N-terminus binding

GOA release 2020-03-11

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GOA release 2020-03-11

author

Gisela Taucher-Scholz

7

object named as

Gisela Taucher-Scholz

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author name string

Olivier J Becherel

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Nuri Gueven

2

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Geoff W Birrell

3

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Valérie Schreiber

4

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Amila Suraweera

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Burkhard Jakob

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Martin F Lavin

Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein

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language of work or name

English

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publication date

15 July 2006

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published in

Human Molecular Genetics

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volume

15

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page(s)

2239-49

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issue

14

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cites work

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The novel human gene aprataxin is directly involved in DNA single-strand-break repair.

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Major nucleolar proteins shuttle between nucleus and cytoplasm

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Nuclear export of proteins: the role of nuclear retention.

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The FHA domain of aprataxin interacts with the C-terminal region of XRCC1

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The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4

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Genetic inactivation of the transcription factor TIF-IA leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis

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The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin

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Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin

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