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Gene Review

SYNPO2  -  synaptopodin 2

Homo sapiens

Synonyms: Genethonin-2, MYOPODIN, Myopodin, Synaptopodin-2


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Disease relevance of SYNPO2


High impact information on SYNPO2

  • Nuclear export of myopodin is sensitive to leptomycin B, despite the absence of a classical nuclear export sequence [2].
  • During myotube differentiation, myopodin binds to stress fibers in a punctuated pattern before incorporation into the Z-disc [2].
  • Myopodin can directly bind to actin and contains a novel actin binding site in the center of the protein [2].
  • Myopodin has actin-bundling activity as shown by formation of latrunculin-A-sensitive cytosolic actin bundles, nuclear actin loops in transfected cells expressing green fluorescent protein-myopodin [2] and electron microscopy [3].
  • In myoblasts, myopodin shows preferential nuclear localization [2].
  • Myopodin is a multiadapter protein interacting with (in addition to F-actin) filamin and alpha-actinin [4].
  • Myopodin is a key component in filamin homeostasis by mediating interactions with the cochaperone BAG3 and Vps18  [5].

Biological context of SYNPO2

  • Myopodin is a key component in tension-induced and chaperone-assisted autophagy
  • Results from non-muscle cells support the hypothesis that myopodin functions as a tumor suppressor gene to limit the growth and to inhibit the metastasis of cancer cells [1].
  • In addition, hemizygous deletion and down-regulation of myopodin expression occur in three aggressive prostate cancer cell lines [1].
  • In a yeast two-hybrid screen a high-affinity interaction of myopodin with zyxin, a molecule known to regulate cell motility and migration, was identified [6].
  • This sequence was mapped to chromosome 4q25 by screening the Genebridge 4 hamster radiation panel with primers specific to this probe, and subsequently identify a 54-kb minimal common deletion region that contains the sequence encoding myopodin [7].
  • Differential nuclear expression for myopodin was identified among bladder cancer cell lines during cell-cycle [8].

Anatomical context of SYNPO2


Associations of SYNPO2 with chemical compounds

  • METHODS: Immunostaining using anti-myopodin antibodies was performed on 746 formalin-fixed paraffin-embedded tissue samples to evaluate the level of myopodin expression in normal and malignant prostatic tissue [11].

Other interactions of SYNPO2


Analytical, diagnostic and therapeutic context of SYNPO2


  1. Expression of myopodin induces suppression of tumor growth and metastasis. Jing, L., Liu, L., Yu, Y.P., Dhir, R., Acquafondada, M., Landsittel, D., Cieply, K., Wells, A., Luo, J.H. Am. J. Pathol. (2004) [Pubmed]
  2. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. Weins, A., Schwarz, K., Faul, C., Barisoni, L., Linke, W.A., Mundel, P. J. Cell Biol. (2001) [Pubmed]
  3. Myopodin is an F-actin bundling protein with multiple independent actin-binding regions. Linnemann, A., Vakeel, P., Bezerra, E., Orfanos, Z., Djinović-Carugo, K., van der Ven, P.F., Kirfel, G., Fürst, D.O. J. Muscle. Res. Cell. Motil. (2013) [Pubmed]
  4. The sarcomeric Z-disc component myopodin is a multiadapter protein that interacts with filamin and alpha-actinin. Linnemann, A., van der Ven, P.F., Vakeel, P., Albinus, B., Simonis, D., Bendas, G., Schenk, J.A., Micheel, B., Kley, R.A., Fürst, D.O. Eur. J. Cell. Biol. (2010) [Pubmed]
  5. Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. Ulbricht, A., Eppler, F.J., Tapia, V.E., van der Ven, P.F., Hampe, N., Hersch, N., Vakeel, P., Stadel, D., Haas, A., Saftig, P., Behrends, C., Fürst, D.O., Volkmer, R., Hoffmann, B., Kolanus, W., Höhfeld, J. Curr. Biol. (2013) [Pubmed]
  6. Myopodin-mediated suppression of prostate cancer cell migration involves interaction with zyxin. Yu, Y.P., Luo, J.H. Cancer Res. (2006) [Pubmed]
  7. Myopodin, a synaptopodin homologue, is frequently deleted in invasive prostate cancers. Lin, F., Yu, Y.P., Woods, J., Cieply, K., Gooding, B., Finkelstein, P., Dhir, R., Krill, D., Becich, M.J., Michalopoulos, G., Finkelstein, S., Luo, J.H. Am. J. Pathol. (2001) [Pubmed]
  8. Tumor suppressor role for myopodin in bladder cancer: loss of nuclear expression of myopodin is cell-cycle dependent and predicts clinical outcome. Sanchez-Carbayo, M., Schwarz, K., Charytonowicz, E., Cordon-Cardo, C., Mundel, P. Oncogene (2003) [Pubmed]
  9. A monopartite nuclear localization sequence regulates nuclear targeting of the actin binding protein myopodin. De Ganck, A., Hubert, T., Van Impe, K., Geelen, D., Vandekerckhove, J., De Corte, V., Gettemans, J. FEBS Lett. (2005) [Pubmed]
  10. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. Weins, A., Schwarz, K., Faul, C., Barisoni, L., Linke, W.A., Mundel, P. J. Cell. Biol. (2001) [Pubmed]
  11. Inactivation of myopodin expression associated with prostate cancer relapse. Yu, Y.P., Tseng, G.C., Luo, J.H. Urology (2006) [Pubmed]
  12. The Nucleo-cytoplasmic actin-binding protein CapG lacks a nuclear export sequence present in structurally related proteins. Van Impe, K., De Corte, V., Eichinger, L., Bruyneel, E., Mareel, M., Vandekerckhove, J., Gettemans, J. J. Biol. Chem. (2003) [Pubmed]
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