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Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain.

Abstract:

The human RNA-editing enzyme adenosine deaminase that acts on RNA (ADAR1) is expressed in two versions. A longer 150-kDa protein is interferon inducible and can be found both in the nucleus and cytoplasm. An amino-terminally truncated 110-kDa version, in contrast, is constitutively expressed and predominantly nuclear. In the absence of transcription, however, the shorter protein is also cytoplasmic and thus displays the hallmarks of a shuttling protein. The nuclear localization signal (NLS) o...

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Publisher copy:
10.1091/mbc.e02-03-0161

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Journal:
Molecular biology of the cell
Volume:
13
Issue:
11
Pages:
3822-3835
Publication date:
2002-11-05
DOI:
EISSN:
1939-4586
ISSN:
1059-1524
URN:
uuid:26a19e2a-8493-43d4-bf01-62692c0cab43
Source identifiers:
334664
Local pid:
pubs:334664

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