Proteopedia

Group:MUZIC:Tritopodin

Prediction of the PDZ binding domain of Tritopodin . Lambert et al. ESyPred3D:Prediction of Proteins 3D structures. Bioinformatics 2002)

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TRITOPODINTRITOPODIN

Tritopodin is the third member (besides myopodin and synaptopodin) of the podin family proteins and is codified by the gene SYNPO2L[1]. Tritopodin has been revealed by database searches, and since it is the third member of a family of proteins with extended sequence similarity, was named ‘‘tritopodin’’. Tritopodin is also known under the names synaptopodin 2-like, Myopodin-like and CHAP (cytoskeletal heart-enriched actin-associated protein), is found in heart and skeletal muscle tissue [1]. Tritopodin share with Myopodin 33% of homology in the Aminoacid sequence, which makes believe similar functions for both proteins. Tritopodin gene it is form by 5 exons and 2 isoforms are postulated: mCHAPa from exon 1,2,3 and 5, as well as mCHAPb that result from a start-codon in exon 4, from which derives two proteins variants of 140kDa (mCHAPa) and 110kDa (mCHAPb) [2].


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FunctionFunction

Tritopodin is expressed in vivo and in vitro in differentiated skeletal- and heart muscle cells, associates with polymerized actin, and is conserved amongst vertebrates, indicating an essential role in muscle function. Furthermore Tritopodin is able to translocate to the nucleus, and plays an important role in skeletal and cardiac muscle development. [3] [4].


Tritopodin InteractionsTritopodin Interactions

Tritopodin as Synaptopodin and Myopodin localizes in the sarcomeric Z-disc, where they interact with α-actinin and Filamin C, verify by CoIPs and yeast two-hybrid assays [5]. Adult skeletal and heart tissue shows the colocalization from mCHAP with α-actinin in the sarcomeric Z-disc and in the nucleus in embrional Cardiomyocytes [6].


File:Tritopodin interaction with Filamin C.jpg


ReferencesReferences

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  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
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