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 and less researched of the podin family proteins and is codified by the gene SYNPO2L. Tritopodin also known under the names synaptopodin 2-like, Myopodin-like and CHAP (cytoskeletal heart-enriched actin-associated protein), is found in heart (Claeys et al. 2009) ^[1] and skeletal muscle tissue (Beqqali et al. 2010) ^[2]. 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 and the two derives proteins are of 140kDa (mCHAPa) und 110kDa (mCHAPb).

FunctionFunction

Tritopodin is expressed in vivo and in vitro in differentiated skeletal- and heart muscle cells (Linnemann 2010; Beqqali et al. 2010).

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 ^[3] (Linnemann et al. 2010) 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 (Beqqali et al. 2010).

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ReferencesReferences

↑ 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
↑ 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
↑ 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

[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

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