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.

Strehblow, A; Hallegger, M; Jantsch, MF

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...

Expand abstract

Actions

Email

Email this record

Send the bibliographic details of this record to your email address.

Your Email
Please enter the email address that the record information will be sent to.

-
Your message (optional)
Please add any additional information to be included within the email.
Cite

Cite this record

APA Style

Strehblow, A., Hallegger, M., & Jantsch, M. F. (2002). 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. Molecular Biology of the Cell, 13(11), 3822–3835.

MLA Style

Strehblow, A., et al. “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.” Molecular Biology of the Cell, vol. 13, no. 11, 2002, pp. 3822–35.

Chicago Style

Strehblow, A, M Hallegger, and MF Jantsch. 2002. “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.” Molecular Biology of the Cell 13 (11): 3822–35.
Tweet
Print