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Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein.

Publication ,  Journal Article
Weins, A; Schwarz, K; Faul, C; Barisoni, L; Linke, WA; Mundel, P
Published in: J Cell Biol
October 29, 2001

We report the cloning and functional characterization of myopodin, the second member of the synaptopodin gene family. Myopodin shows no significant homology to any known protein except synaptopodin. Northern blot analysis resulted in a 3.6-kb transcript for mouse skeletal and heart muscle. Western blots showed an 80-kD signal for skeletal and a 95-kD signal for heart muscle. Myopodin contains one PPXY motif and multiple PXXP motifs. Myopodin colocalizes with alpha-actinin and is found at the Z-disc as shown by immunogold electron microscopy. In myoblasts, myopodin shows preferential nuclear localization. During myotube differentiation, myopodin binds to stress fibers in a punctuated pattern before incorporation into the Z-disc. Myopodin can directly bind to actin and contains a novel actin binding site in the center of the protein. Myopodin has actin-bundling activity as shown by formation of latrunculin-A-sensitive cytosolic actin bundles and nuclear actin loops in transfected cells expressing green fluorescent protein-myopodin. Under stress conditions, myopodin accumulates in the nucleus and is depleted from the cytoplasm. Nuclear export of myopodin is sensitive to leptomycin B, despite the absence of a classical nuclear export sequence. We propose a dual role for myopodin as a structural protein also participating in signaling pathways between the Z-disc and the nucleus.

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Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

October 29, 2001

Volume

155

Issue

3

Start / End Page

393 / 404

Location

United States

Related Subject Headings

  • Thiazolidines
  • Thiazoles
  • Stress, Physiological
  • Sequence Homology, Amino Acid
  • Recombinant Fusion Proteins
  • RNA, Messenger
  • Protein Transport
  • Nuclear Localization Signals
  • Myocardium
  • Mutagenesis
 

Citation

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Weins, A., Schwarz, K., Faul, C., Barisoni, L., Linke, W. A., & Mundel, P. (2001). Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol, 155(3), 393–404. https://doi.org/10.1083/jcb.200012039
Weins, A., K. Schwarz, C. Faul, L. Barisoni, W. A. Linke, and P. Mundel. “Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein.J Cell Biol 155, no. 3 (October 29, 2001): 393–404. https://doi.org/10.1083/jcb.200012039.
Weins A, Schwarz K, Faul C, Barisoni L, Linke WA, Mundel P. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol. 2001 Oct 29;155(3):393–404.
Weins, A., et al. “Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein.J Cell Biol, vol. 155, no. 3, Oct. 2001, pp. 393–404. Pubmed, doi:10.1083/jcb.200012039.
Weins A, Schwarz K, Faul C, Barisoni L, Linke WA, Mundel P. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol. 2001 Oct 29;155(3):393–404.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

October 29, 2001

Volume

155

Issue

3

Start / End Page

393 / 404

Location

United States

Related Subject Headings

  • Thiazolidines
  • Thiazoles
  • Stress, Physiological
  • Sequence Homology, Amino Acid
  • Recombinant Fusion Proteins
  • RNA, Messenger
  • Protein Transport
  • Nuclear Localization Signals
  • Myocardium
  • Mutagenesis