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A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin

Ariane De Ganck (UGent) , Thomas Hubert (UGent) , Katrien Van Impe (UGent) , Danny Geelen (UGent) , Joël Vandekerckhove (UGent) , Veerle De Corte (UGent) and Jan Gettemans (UGent)
(2005) FEBS LETTERS. 579(29). p.6673-6680
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Abstract
Myopodin is an actin bundling protein that shuttles between nucleus and cytoplasm in response to cell stress or during differentiation. Here, we show that the myopodin sequence (58)KKRRRRARK(66), when tagged to either enhanced green fluorescent protein (EGFP) or to enhanced cyan fluorescent protein-CapG (ECFPCapG), is able to target these proteins to the nucleolus in HeLa or H-EK293T cells. By contrast, (KKRR61)-K-58 ECFP-CapG accumulates in the nucleus. Mutation of (58)KKRRRRARK(66) into alanine residues blocks myopodin nuclear import and promotes formation of cytoplasmic actin filaments. A second putative nuclear localization sequence, (612)KTSKKKGKK(620), displays much weaker activity in a heterologous context, and appears not to be functional in the full length protein. Thus myopodin nuclear translocation is dependent on a monopartite nuclear localization sequence.

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Chicago
De Ganck, Ariane, Thomas Hubert, Katrien Van Impe, Danny Geelen, Joël Vandekerckhove, Veerle De Corte, and Jan Gettemans. 2005. “A Monopartite Nuclear Localization Sequence Regulates Nuclear Targeting of the Actin Binding Protein Myopodin.” Febs Letters 579 (29): 6673–6680.
APA
De Ganck, A., Hubert, T., Van Impe, K., Geelen, D., Vandekerckhove, J., De Corte, V., & Gettemans, J. (2005). A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin. FEBS LETTERS, 579(29), 6673–6680.
Vancouver
1.
De Ganck A, Hubert T, Van Impe K, Geelen D, Vandekerckhove J, De Corte V, et al. A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin. FEBS LETTERS. Elsevier Science; 2005;579(29):6673–80.
MLA
De Ganck, Ariane et al. “A Monopartite Nuclear Localization Sequence Regulates Nuclear Targeting of the Actin Binding Protein Myopodin.” FEBS LETTERS 579.29 (2005): 6673–6680. Print.
@article{324465,
  abstract     = {Myopodin is an actin bundling protein that shuttles between nucleus and cytoplasm in response to cell stress or during differentiation. Here, we show that the myopodin sequence (58)KKRRRRARK(66), when tagged to either enhanced green fluorescent protein (EGFP) or to enhanced cyan fluorescent protein-CapG (ECFPCapG), is able to target these proteins to the nucleolus in HeLa or H-EK293T cells. By contrast, (KKRR61)-K-58 ECFP-CapG accumulates in the nucleus. Mutation of (58)KKRRRRARK(66) into alanine residues blocks myopodin nuclear import and promotes formation of cytoplasmic actin filaments. A second putative nuclear localization sequence, (612)KTSKKKGKK(620), displays much weaker activity in a heterologous context, and appears not to be functional in the full length protein. Thus myopodin nuclear translocation is dependent on a monopartite nuclear localization sequence.},
  author       = {De Ganck, Ariane and Hubert, Thomas and Van Impe, Katrien and Geelen, Danny and Vandekerckhove, Jo{\"e}l and De Corte, Veerle and Gettemans, Jan},
  issn         = {0014-5793},
  journal      = {FEBS LETTERS},
  language     = {eng},
  number       = {29},
  pages        = {6673--6680},
  publisher    = {Elsevier Science},
  title        = {A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin},
  url          = {http://dx.doi.org/10.1016/j.febslet.2005.10.054},
  volume       = {579},
  year         = {2005},
}

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