A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin |
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Authors: | De Ganck Ariane Hubert Thomas Van Impe Katrien Geelen Danny Vandekerckhove Joël De Corte Veerle Gettemans Jan |
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Institution: | Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (V.I.B.), Ghent University, Faculty of Medicine and Health Sciences, Albert Baertsoenkaai 3, B-9000 Ghent, Belgium. |
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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 58KKRRRRARK66, 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 HEK293T cells. By contrast, 58KKRR61-ECFP-CapG accumulates in the nucleus. Mutation of 58KKRRRRARK66 into alanine residues blocks myopodin nuclear import and promotes formation of cytoplasmic actin filaments. A second putative nuclear localization sequence, 612KTSKKKGKK620, 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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Keywords: | β-gal beta-galactosidase ECFP enhanced cyan fluorescent protein EGFP enhanced green fluorescent protein NLS nuclear localization sequence |
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