Group:MUZIC:Synaptopodin

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== Introduction ==
== Introduction ==
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Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find also [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>. The last member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.
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Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.
== Sequence annotation ==
== Sequence annotation ==

Revision as of 15:09, 17 January 2013

Contents

Introduction

Synaptopodin, a protein encoded by the gene SYNPO,and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent [1] [2]. Synaptopodin is either a member of the podin family, where we can find myopodin, present in avian smooth muscle (Leinweber et al. 1999)[3] heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)[4], and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names tritopodin (Claeys et al. 2009)[5] or CHAP (Beqqali et al. 2010)[6].

Sequence annotation

Image:Synaptopodin isoform.png
Synaptopodin isoforms

Structure

There is no structure related for this protein.

Function and interactions

Is described an interaction between synaptopodin and alpha-actinin as myopodin, which contains a alpha-actinin-binding site that shows high homology to the podin family members with a conserved filamin binding region(Linnemann et al. 2010)[7].Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity. synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration [8]. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting [9].

Pathology

References

  1. ↑ Mundel P, Heid HW, Mundel TM, Kruger M, Reiser J, Kriz W. Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes. J Cell Biol. 1997 Oct 6;139(1):193-204. PMID:9314539
  2. ↑ Deller T, Merten T, Roth SU, Mundel P, Frotscher M. Actin-associated protein synaptopodin in the rat hippocampal formation: localization in the spine neck and close association with the spine apparatus of principal neurons. J Comp Neurol. 2000 Mar 6;418(2):164-81. PMID:10701442
  3. ↑ Leinweber BD, Fredricksen RS, Hoffman DR, Chalovich JM. Fesselin: a novel synaptopodin-like actin binding protein from muscle tissue. J Muscle Res Cell Motil. 1999 Aug;20(5-6):539-45. PMID:10555072
  4. ↑ 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. Epub 2001 Oct 22. PMID:11673475 doi:10.1083/jcb.200012039
  5. ↑ Claeys KG, van der Ven PF, Behin A, Stojkovic T, Eymard B, Dubourg O, Laforet P, Faulkner G, Richard P, Vicart P, Romero NB, Stoltenburg G, Udd B, Fardeau M, Voit T, Furst DO. Differential involvement of sarcomeric proteins in myofibrillar myopathies: a morphological and immunohistochemical study. Acta Neuropathol. 2009 Mar;117(3):293-307. Epub 2009 Jan 17. PMID:19151983 doi:10.1007/s00401-008-0479-7
  6. ↑ Beqqali A, Monshouwer-Kloots J, Monteiro R, Welling M, Bakkers J, Ehler E, Verkleij A, Mummery C, Passier R. CHAP is a newly identified Z-disc protein essential for heart and skeletal muscle function. J Cell Sci. 2010 Apr 1;123(Pt 7):1141-50. Epub 2010 Mar 9. PMID:20215401 doi:10.1242/jcs.063859
  7. ↑ Linnemann A, van der Ven PF, Vakeel P, Albinus B, Simonis D, Bendas G, Schenk JA, Micheel B, Kley RA, Furst DO. The sarcomeric Z-disc component myopodin is a multiadapter protein that interacts with filamin and alpha-actinin. Eur J Cell Biol. 2010 Sep;89(9):681-92. Epub 2010 May 31. PMID:20554076 doi:10.1016/j.ejcb.2010.04.004
  8. ↑ Asanuma K, Yanagida-Asanuma E, Faul C, Tomino Y, Kim K, Mundel P. Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat Cell Biol. 2006 May;8(5):485-91. Epub 2006 Apr 16. PMID:16622418 doi:10.1038/ncb1400
  9. ↑ Roth SU, Sommer C, Mundel P, Kiessling M. Expression of synaptopodin, an actin-associated protein, in the rat hippocampus after limbic epilepsy. Brain Pathol. 2001 Apr;11(2):169-81. PMID:11303792

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