Skip Navigation


Nucleic Acids Research Advance Access first published online on September 20, 2006
This version published online on October 6, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl659
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (5613K) Freely available
Right arrow Screen PDF (695K) Freely available
Right arrowOA All Versions of this Article:
34/18/5060    most recent
gkl659v3
gkl659v2
gkl659v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Smaldone, S.
Right arrow Articles by Ramirez, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smaldone, S.
Right arrow Articles by Ramirez, F.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Multiple pathways regulate intracellular shuttling of MoKA, a co-activator of transcription factor KLF7

Silvia Smaldone and Francesco Ramirez*

Child Health Institute of New Jersey, Robert W. Johnson Medical School 89 French Street, New Brunswick, NJ 08901, USA CEINGE Biotecnologie Avanzate 80131 Naples, Italy

*To whom correspondence should be addressed. Tel: +1 732 235 9534; Fax: +1 732 235 9333; Email: ramirefr{at}umdnj.edu

Received April 5, 2006. Revised June 15, 2006. Accepted August 28, 2006.

MoKA is a novel F-box containing protein that interacts with and stimulates the activity of transcription factor KLF7, a regulator of neuronal differentiation. MoKA accumulates throughout the cell and predominantly in the cytosol, consistent with the presence of several putative nuclear localization and export signals (NLSs and NESs). The present study was designed to refine the identity and location of the sequences responsible for MoKA intracellular shuttling and transcriptional activity. Forced expression of fusion proteins in mammalian cells demonstrated that only one of three putative NLSs potentially recognized by karyopherin receptors is involved in nuclear localization of MoKA. By contrast, three distinct sequences were found to participate in mediating cytoplasmic accumulation. One of them is structurally and functionally related to the leucine-rich export signal that interacts with the exportin 1 (CRM1) receptor. The other two export signals instead display either a novel leucine-rich sequence or an undefined peptide motif, and both appear to act through CRM1-independent pathways. Finally, transcriptional analyses using the chimeric GAL4 system mapped the major activation domain of MoKA to a highly acidic sequence that resides between the NLS and NES clusters.

The history dates have been corrected.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.