{{Short description|Protein in the human body}} {{Infobox_gene}} '''Telethonin''', also known as '''Tcap''', is a protein that in humans is encoded by the ''TCAP'' gene.<ref name="pmid9350988">{{cite journal | vauthors = Valle G, Faulkner G, De Antoni A, Pacchioni B, Pallavicini A, Pandolfo D, Tiso N, Toppo S, Trevisan S, Lanfranchi G | title = Telethonin, a novel sarcomeric protein of heart and skeletal muscle | journal = FEBS Letters | volume = 415 | issue = 2 | pages = 163–8 | date = Sep 1997 | pmid = 9350988 | doi = 10.1016/S0014-5793(97)01108-3 | s2cid = 1482856 | doi-access = free | hdl = 11577/2469154 | hdl-access = free }}</ref><ref name="pmid9817758">{{cite journal | vauthors = Gregorio CC, Trombitás K, Centner T, Kolmerer B, Stier G, Kunke K, Suzuki K, Obermayr F, Herrmann B, Granzier H, Sorimachi H, Labeit S | title = The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity | journal = The Journal of Cell Biology | volume = 143 | issue = 4 | pages = 1013–27 | date = Nov 1998 | pmid = 9817758 | pmc = 2132961 | doi = 10.1083/jcb.143.4.1013 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TCAP titin-cap (telethonin)| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8557}}</ref> Telethonin is expressed in cardiac and skeletal muscle at Z-discs and functions to regulate sarcomere assembly, T-tubule function and apoptosis. Telethonin has been implicated in several diseases, including limb-girdle muscular dystrophy, hypertrophic cardiomyopathy, dilated cardiomyopathy and idiopathic cardiomyopathy.
==Structure== Telethonin is a 19.0 kDa protein composed of 167 amino acids.<ref>{{cite web|title=Protein Information for the human TCAP gene (Uniprot ID: O15273)|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=O15273|website=COPaKB: Cardiac Organellar Protein Atlas Knowledgebase|access-date=20 June 2015}}{{Dead link|date=August 2025 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> Telethonin has a unique β-sheet structure, which enables antiparallel association with the Titin Z1-Z2 domains in cardiac and skeletal muscle.<ref>{{cite journal | vauthors = Zou P, Pinotsis N, Lange S, Song YH, Popov A, Mavridis I, Mayans OM, Gautel M, Wilmanns M | title = Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk | journal = Nature | volume = 439 | issue = 7073 | pages = 229–33 | date = Jan 2006 | pmid = 16407954 | doi = 10.1038/nature04343 | bibcode = 2006Natur.439..229Z | s2cid = 7509846 | url = http://bib-pubdb1.desy.de/record/80904 }}</ref> Structural analysis of full-length Telethonin with the N-terminal region of Titin indicate that the C-terminus of Telethonin is critical for the dimerization of two Telethonin/Titin complexes into a higher oligomeric structure.<ref>{{cite journal | vauthors = Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M | title = Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus | journal = Journal of Structural Biology | volume = 155 | issue = 2 | pages = 239–50 | date = Aug 2006 | pmid = 16713295 | doi = 10.1016/j.jsb.2006.03.028 }}</ref>
== Function == Telethonin expression is developmentally regulated in both cardiac and skeletal muscle and is thought to be critical to sarcomere assembly.<ref>{{cite journal | vauthors = Mason P, Bayol S, Loughna PT | title = The novel sarcomeric protein telethonin exhibits developmental and functional regulation | journal = Biochemical and Biophysical Research Communications | volume = 257 | issue = 3 | pages = 699–703 | date = Apr 1999 | pmid = 10208846 | doi = 10.1006/bbrc.1999.0531 }}</ref> Telethonin was found to be a late assembling protein only present in mature myofibrils at Z-discs.<ref>{{cite journal | vauthors = White J, Barro MV, Makarenkova HP, Sanger JW, Sanger JM | title = Localization of sarcomeric proteins during myofibril assembly in cultured mouse primary skeletal myotubes | journal = Anatomical Record | volume = 297 | issue = 9 | pages = 1571–84 | date = Sep 2014 | pmid = 25125171 | doi = 10.1002/ar.22981 | pmc=4145531}}</ref>
Telethonin forms a complex with muscle LIM protein (MLP) at sarcomere Z-discs, which constitutes part of the cardiomyocyte stretch sensory mechanism.<ref name="ReferenceA">{{cite journal | vauthors = Knöll R, Hoshijima M, Hoffman HM, Person V, Lorenzen-Schmidt I, Bang ML, Hayashi T, Shiga N, Yasukawa H, Schaper W, McKenna W, Yokoyama M, Schork NJ, Omens JH, McCulloch AD, Kimura A, Gregorio CC, Poller W, Schaper J, Schultheiss HP, Chien KR | title = The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy | journal = Cell | volume = 111 | issue = 7 | pages = 943–55 | date = Dec 2002 | pmid = 12507422 | doi=10.1016/s0092-8674(02)01226-6| s2cid = 15082967 | doi-access = free }}</ref> It has also been shown that Telethonin binds to the beta-subunit of the slow activating component of the delayed rectifier potassium channel, MinK, in areas localized to T-tubule membranes surrounding Z-lines in the inner myocardium.<ref name="Furukawa T 2001">{{cite journal | vauthors = Furukawa T, Ono Y, Tsuchiya H, Katayama Y, Bang ML, Labeit D, Labeit S, Inagaki N, Gregorio CC | title = Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system | journal = Journal of Molecular Biology | volume = 313 | issue = 4 | pages = 775–84 | date = Nov 2001 | pmid = 11697903 | doi = 10.1006/jmbi.2001.5053 }}</ref> In addition, Telethonin interacts with the sodium channel Na(v)1.5, and alters the activation kinetics via doubling the window current.<ref name="ReferenceB">{{cite journal | vauthors = Mazzone A, Strege PR, Tester DJ, Bernard CE, Faulkner G, De Giorgio R, Makielski JC, Stanghellini V, Gibbons SJ, Ackerman MJ, Farrugia G | title = A mutation in telethonin alters Nav1.5 function | journal = The Journal of Biological Chemistry | volume = 283 | issue = 24 | pages = 16537–44 | date = Jun 2008 | pmid = 18408010 | doi = 10.1074/jbc.M801744200 | pmc=2423252| doi-access = free }}</ref> These data suggest that Telethonin may constitute a mechano-electrical links between Z-lines and T-tubules. Further functional evidence for this has come from studies utilizing a Telethonin-knockout mouse (KO), which have shown that Telethonin is involved in T-tubule structure and function, as well as apoptosis in the heart. Telethonin KO animals showed preserved Titin anchoring at baseline, and instead showed a profound deficit during nuclear biomechanical stress in modulating the turnover of the proapoptotic p53 protein.<ref>{{cite journal | vauthors = Knöll R, Linke WA, Zou P, Miocic S, Kostin S, Buyandelger B, Ku CH, Neef S, Bug M, Schäfer K, Knöll G, Felkin LE, Wessels J, Toischer K, Hagn F, Kessler H, Didié M, Quentin T, Maier LS, Teucher N, Unsöld B, Schmidt A, Birks EJ, Gunkel S, Lang P, Granzier H, Zimmermann WH, Field LJ, Faulkner G, Dobbelstein M, Barton PJ, Sattler M, Wilmanns M, Chien KR | title = Telethonin deficiency is associated with maladaptation to biomechanical stress in the mammalian heart | journal = Circulation Research | volume = 109 | issue = 7 | pages = 758–69 | date = Sep 2011 | pmid = 21799151 | doi = 10.1161/CIRCRESAHA.111.245787 | pmc=3664427}}</ref> Telethonin KO animals also displayed calcium transient dysynchrony, T-tubule loss and depressed L-type calcium channel function.<ref>{{cite journal | vauthors = Ibrahim M, Siedlecka U, Buyandelger B, Harada M, Rao C, Moshkov A, Bhargava A, Schneider M, Yacoub MH, Gorelik J, Knöll R, Terracciano CM | title = A critical role for Telethonin in regulating t-tubule structure and function in the mammalian heart | journal = Human Molecular Genetics | volume = 22 | issue = 2 | pages = 372–83 | date = Jan 2013 | pmid = 23100327 | doi = 10.1093/hmg/dds434 | pmc=3526164}}</ref>
Telethonin is a substrate of titin kinase,<ref name="pmid9804419"/> protein kinase D (PKD) and CaM Kinase II.<ref name="ReferenceC">{{cite journal | vauthors = Candasamy AJ, Haworth RS, Cuello F, Ibrahim M, Aravamudhan S, Krüger M, Holt MR, Terracciano CM, Mayr M, Gautel M, Avkiran M | title = Phosphoregulation of the titin-cap protein telethonin in cardiac myocytes | journal = The Journal of Biological Chemistry | volume = 289 | issue = 3 | pages = 1282–93 | date = Jan 2014 | pmid = 24280220 | doi = 10.1074/jbc.M113.479030 | pmc=3894314| doi-access = free }}</ref> Telethonin, as well as TNNI3, MYBPC3 and MYOM2 are phosphorylated by PKD in cardiomyocytes, and this leads to a reduction in calcium sensitivity of myofilaments, as well as accelerated crossbridge kinetics.<ref>{{cite journal | vauthors = Haworth RS, Cuello F, Herron TJ, Franzen G, Kentish JC, Gautel M, Avkiran M | title = Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function | journal = Circulation Research | volume = 95 | issue = 11 | pages = 1091–9 | date = Nov 2004 | pmid = 15514163 | doi = 10.1161/01.RES.0000149299.34793.3c | doi-access = free }}</ref> Bis-phosphorylation of Telethonin specifically at sites Serine-157 and Serine-161 has been shown to be essential for normal T-tubule organization and intracellular calcium transient kinetics.<ref name="ReferenceC"/>
The intracellular degradation of Telethonin is regulated by MDM2 in a proteasomal-dependent yet ubiquitin-independent manner.<ref>{{cite journal | vauthors = Tian LF, Li HY, Jin BF, Pan X, Man JH, Zhang PJ, Li WH, Liang B, Liu H, Zhao J, Gong WL, Zhou T, Zhang XM | title = MDM2 interacts with and downregulates a sarcomeric protein, TCAP | journal = Biochemical and Biophysical Research Communications | volume = 345 | issue = 1 | pages = 355–61 | date = Jun 2006 | pmid = 16678796 | doi = 10.1016/j.bbrc.2006.04.108 }}.</ref> Telethonin specifically interacts with the pro-apoptotic protein Siva, suggesting that Telethonin may be involved in the mechanism underlying Coxsackievirus B3 infection in acute and chronic myocarditis<ref>{{cite journal | vauthors = Mihatsch K, Nestler M, Saluz HP, Henke A, Munder T | title = Proapoptotic protein Siva binds to the muscle protein telethonin in cardiomyocytes during coxsackieviral infection | journal = Cardiovascular Research | volume = 81 | issue = 1 | pages = 108–15 | date = Jan 2009 | pmid = 18849585 | doi = 10.1093/cvr/cvn276 | doi-access = free }}</ref>
Telethonin was also identified to be targeted and regulated by transcriptional activators CLOCK and BMAL1, thus demonstrating that ''TCAP'' is a circadian regulated gene.<ref>{{cite journal | vauthors = Podobed PS, Alibhai FJ, Chow CW, Martino TA | title = Circadian regulation of myocardial sarcomeric Titin-cap (Tcap, telethonin): identification of cardiac clock-controlled genes using open access bioinformatics data | journal = PLOS ONE | volume = 9 | issue = 8 | article-number = e104907 | date = 2014 | pmid = 25121604 | doi = 10.1371/journal.pone.0104907 | pmc=4133362| bibcode = 2014PLoSO...9j4907P | doi-access = free }}</ref>
==Clinical Significance== Mutations in this gene are associated with limb-girdle muscular dystrophy type R7 (previously 2G),<ref>{{cite journal | vauthors = Vainzof M, Moreira ES, Suzuki OT, Faulkner G, Valle G, Beggs AH, Carpen O, Ribeiro AF, Zanoteli E, Gurgel-Gianneti J, Tsanaclis AM, Silva HC, Passos-Bueno MR, Zatz M | title = Telethonin protein expression in neuromuscular disorders | journal = Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | volume = 1588 | issue = 1 | pages = 33–40 | date = Oct 2002 | pmid = 12379311 | doi=10.1016/s0925-4439(02)00113-8| url = http://repositorio.unifesp.br/handle/11600/27000 | doi-access = free | url-access = subscription }}</ref> hypertrophic cardiomyopathy,<ref>{{cite journal | vauthors = Andersen PS, Havndrup O, Hougs L, Sørensen KM, Jensen M, Larsen LA, Hedley P, Thomsen AR, Moolman-Smook J, Christiansen M, Bundgaard H | title = Diagnostic yield, interpretation, and clinical utility of mutation screening of sarcomere encoding genes in Danish hypertrophic cardiomyopathy patients and relatives | journal = Human Mutation | volume = 30 | issue = 3 | pages = 363–70 | date = Mar 2009 | pmid = 19035361 | doi = 10.1002/humu.20862 | s2cid = 30898294 }}</ref><ref>{{cite journal | vauthors = Bos JM, Poley RN, Ny M, Tester DJ, Xu X, Vatta M, Towbin JA, Gersh BJ, Ommen SR, Ackerman MJ | title = Genotype-phenotype relationships involving hypertrophic cardiomyopathy-associated mutations in titin, muscle LIM protein, and telethonin | journal = Molecular Genetics and Metabolism | volume = 88 | issue = 1 | pages = 78–85 | date = May 2006 | pmid = 16352453 | doi = 10.1016/j.ymgme.2005.10.008 | pmc=2756511}}</ref><ref>{{cite journal | vauthors = Theis JL, Bos JM, Bartleson VB, Will ML, Binder J, Vatta M, Towbin JA, Gersh BJ, Ommen SR, Ackerman MJ | title = Echocardiographic-determined septal morphology in Z-disc hypertrophic cardiomyopathy | journal = Biochemical and Biophysical Research Communications | volume = 351 | issue = 4 | pages = 896–902 | date = Dec 2006 | pmid = 17097056 | doi = 10.1016/j.bbrc.2006.10.119 }}</ref> dilated cardiomyopathy,<ref>{{cite journal | vauthors = Rampersaud E, Siegfried JD, Norton N, Li D, Martin E, Hershberger RE | title = Rare variant mutations identified in pediatric patients with dilated cardiomyopathy | journal = Progress in Pediatric Cardiology | volume = 31 | issue = 1 | pages = 39–47 | date = Jan 2011 | pmid = 21483645 | doi = 10.1016/j.ppedcard.2010.11.008 | pmc=3072577}}</ref><ref>{{cite journal | vauthors = Hirtle-Lewis M, Desbiens K, Ruel I, Rudzicz N, Genest J, Engert JC, Giannetti N | title = The genetics of dilated cardiomyopathy: a prioritized candidate gene study of LMNA, TNNT2, TCAP, and PLN | journal = Clinical Cardiology | volume = 36 | issue = 10 | pages = 628–33 | date = Oct 2013 | pmid = 24037902 | doi = 10.1002/clc.22193 | pmc = 6649360 }}</ref> idiopathic cardiomyopathy,<ref>{{cite journal | vauthors = Hershberger RE, Parks SB, Kushner JD, Li D, Ludwigsen S, Jakobs P, Nauman D, Burgess D, Partain J, Litt M | title = Coding sequence mutations identified in MYH7, TNNT2, SCN5A, CSRP3, LBD3, and TCAP from 313 patients with familial or idiopathic dilated cardiomyopathy | journal = Clinical and Translational Science | volume = 1 | issue = 1 | pages = 21–6 | date = May 2008 | pmid = 19412328 | doi = 10.1111/j.1752-8062.2008.00017.x | pmc=2633921}}</ref> and gastrointestinal smooth muscle-related diseases.<ref name="ReferenceB"/>
Two mutations in Telethonin, Thr137Ile and Arg153His have been associated with hypertrophic cardiomyopathy, which enhance the binding of Telethonin with Titin and MYOZ2. The Glu132Gln mutation has been associated with dilated cardiomyopathy, which has the opposite effect in that it impairs the binding of Telethonin with Titin and MYOZ2.<ref>{{cite journal | vauthors = Hayashi T, Arimura T, Itoh-Satoh M, Ueda K, Hohda S, Inagaki N, Takahashi M, Hori H, Yasunami M, Nishi H, Koga Y, Nakamura H, Matsuzaki M, Choi BY, Bae SW, You CW, Han KH, Park JE, Knöll R, Hoshijima M, Chien KR, Kimura A | title = Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy | journal = Journal of the American College of Cardiology | volume = 44 | issue = 11 | pages = 2192–201 | date = Dec 2004 | pmid = 15582318 | doi = 10.1016/j.jacc.2004.08.058 | doi-access = free }}</ref> Mutations in Titin associated with dilated cardiomyopathy, including Val54Met, have been shown specifically to impair binding of Titin with Telethonin.<ref>{{cite journal | vauthors = Itoh-Satoh M, Hayashi T, Nishi H, Koga Y, Arimura T, Koyanagi T, Takahashi M, Hohda S, Ueda K, Nouchi T, Hiroe M, Marumo F, Imaizumi T, Yasunami M, Kimura A | s2cid = 1824336 | title = Titin mutations as the molecular basis for dilated cardiomyopathy | journal = Biochemical and Biophysical Research Communications | volume = 291 | issue = 2 | pages = 385–93 | date = Feb 2002 | pmid = 11846417 | doi = 10.1006/bbrc.2002.6448 }}</ref> In a mouse model of dilated cardiomyopathy, recapitulating the human dilated cardiomyopathy mutation in MLP, Trp4Arg, studies have found that this mutation disrupts normal binding and localization of MLP with Telethonin.<ref name="ReferenceA"/> In a rat model of hypertension-induced cardiomyopathy, a human variant of BMP10, Thr326Ile, showed decreased binding to Telethonin and increased extracellular secretion.<ref>{{cite journal | vauthors = Nakano N, Hori H, Abe M, Shibata H, Arimura T, Sasaoka T, Sawabe M, Chida K, Arai T, Nakahara K, Kubo T, Sugimoto K, Katsuya T, Ogihara T, Doi Y, Izumi T, Kimura A | title = Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 293 | issue = 6 | pages = H3396–403 | date = Dec 2007 | pmid = 17921333 | doi = 10.1152/ajpheart.00311.2007 | s2cid = 45084505 }}</ref>
== Interactions ==
Telethonin has been shown to interact with: {{div col|colwidth=20em}} * ANKRD2,<ref name = pmid15136035>{{cite journal | vauthors = Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G | title = The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle | journal = Journal of Molecular Biology | volume = 339 | issue = 2 | pages = 313–25 | date = May 2004 | pmid = 15136035 | doi = 10.1016/j.jmb.2004.03.071 }}</ref> * BMP10,<ref>{{cite journal | vauthors = Nakano N, Hori H, Abe M, Shibata H, Arimura T, Sasaoka T, Sawabe M, Chida K, Arai T, Nakahara K, Kubo T, Sugimoto K, Katsuya T, Ogihara T, Doi Y, Izumi T, Kimura A | title = Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 293 | issue = 6 | pages = H3396–403 | date = Dec 2007 | pmid = 17921333 | doi = 10.1152/ajpheart.00311.2007 | s2cid = 45084505 }}</ref> * MLP,<ref name="ReferenceA"/> * MinK,<ref name="Furukawa T 2001"/> * MDM2,<ref>{{cite journal | vauthors = Tian LF, Li HY, Jin BF, Pan X, Man JH, Zhang PJ, Li WH, Liang B, Liu H, Zhao J, Gong WL, Zhou T, Zhang XM | title = MDM2 interacts with and downregulates a sarcomeric protein, TCAP | journal = Biochemical and Biophysical Research Communications | volume = 345 | issue = 1 | pages = 355–61 | date = Jun 2006 | pmid = 16678796 | doi = 10.1016/j.bbrc.2006.04.108 }}</ref> * MSTN,<ref>{{cite journal | vauthors = Nicholas G, Thomas M, Langley B, Somers W, Patel K, Kemp CF, Sharma M, Kambadur R | title = Titin-cap associates with, and regulates secretion of, Myostatin | journal = Journal of Cellular Physiology | volume = 193 | issue = 1 | pages = 120–31 | date = Oct 2002 | pmid = 12209887 | doi = 10.1002/jcp.10158 | s2cid = 8866409 | url = http://researchonline.rvc.ac.uk/id/eprint/1181/ | url-access = subscription }}</ref> * MYOZ1,<ref name = pmid11842093>{{cite journal | vauthors = Frey N, Olson EN | title = Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins | journal = The Journal of Biological Chemistry | volume = 277 | issue = 16 | pages = 13998–4004 | date = Apr 2002 | pmid = 11842093 | doi = 10.1074/jbc.M200712200 | doi-access = free }}</ref><ref name = pmid10984498>{{cite journal | vauthors = Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G | title = FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle | journal = The Journal of Biological Chemistry | volume = 275 | issue = 52 | pages = 41234–42 | date = Dec 2000 | pmid = 10984498 | doi = 10.1074/jbc.M007493200 | doi-access = free | hdl = 11368/1698365 | hdl-access = free }}</ref> * MYOZ2,<ref name="pmid11842093"/> * PRKD1,<ref>{{cite journal | vauthors = Haworth RS, Cuello F, Herron TJ, Franzen G, Kentish JC, Gautel M, Avkiran M | title = Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function | journal = Circulation Research | volume = 95 | issue = 11 | pages = 1091–9 | date = Nov 2004 | pmid = 15514163 | doi = 10.1161/01.RES.0000149299.34793.3c | doi-access = free }}</ref> * SCN5A,<ref name="ReferenceB"/> * SIVA,<ref>{{cite journal | vauthors = Mihatsch K, Nestler M, Saluz HP, Henke A, Munder T | title = Proapoptotic protein Siva binds to the muscle protein telethonin in cardiomyocytes during coxsackieviral infection | journal = Cardiovascular Research | volume = 81 | issue = 1 | pages = 108–15 | date = Jan 2009 | pmid = 18849585 | doi = 10.1093/cvr/cvn276 | doi-access = free }}</ref> and * Titin,<ref name = pmid9817758/><ref name = pmid9804419>{{cite journal | vauthors = Mayans O, van der Ven PF, Wilm M, Mues A, Young P, Fürst DO, Wilmanns M, Gautel M | title = Structural basis for activation of the titin kinase domain during myofibrillogenesis | journal = Nature | volume = 395 | issue = 6705 | pages = 863–9 | date = Oct 1998 | pmid = 9804419 | doi = 10.1038/27603 | bibcode = 1998Natur.395..863M | s2cid = 4426977 }}</ref><ref name = pmid12446666>{{cite journal | vauthors = Zou P, Gautel M, Geerlof A, Wilmanns M, Koch MH, Svergun DI | title = Solution scattering suggests cross-linking function of telethonin in the complex with titin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 4 | pages = 2636–44 | date = Jan 2003 | pmid = 12446666 | doi = 10.1074/jbc.M210217200 | doi-access = free }}</ref><ref name = pmid9645487>{{cite journal | vauthors = Mues A, van der Ven PF, Young P, Fürst DO, Gautel M | title = Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin | journal = FEBS Letters | volume = 428 | issue = 1–2 | pages = 111–4 | date = May 1998 | pmid = 9645487 | doi = 10.1016/s0014-5793(98)00501-8| s2cid = 11786578 | doi-access = free }}</ref> {{Div col end}}
== References == {{reflist|33em}}
== Further reading == {{refbegin|33em}} * {{cite journal | vauthors = Faulkner G, Lanfranchi G, Valle G | title = Telethonin and other new proteins of the Z-disc of skeletal muscle | journal = IUBMB Life | volume = 51 | issue = 5 | pages = 275–82 | date = May 2001 | pmid = 11699871 | doi = 10.1080/152165401317190761 | s2cid = 23688131 | doi-access = free }} * {{cite journal | vauthors = Moreira ES, Vainzof M, Marie SK, Sertié AL, Zatz M, Passos-Bueno MR | title = The seventh form of autosomal recessive limb-girdle muscular dystrophy is mapped to 17q11-12 | journal = American Journal of Human Genetics | volume = 61 | issue = 1 | pages = 151–9 | date = Jul 1997 | pmid = 9245996 | pmc = 1715843 | doi = 10.1086/513889 }} * {{cite journal | vauthors = Mues A, van der Ven PF, Young P, Fürst DO, Gautel M | title = Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin | journal = FEBS Letters | volume = 428 | issue = 1–2 | pages = 111–4 | date = May 1998 | pmid = 9645487 | doi = 10.1016/S0014-5793(98)00501-8 | s2cid = 11786578 | doi-access = free }} * {{cite journal | vauthors = Mayans O, van der Ven PF, Wilm M, Mues A, Young P, Fürst DO, Wilmanns M, Gautel M | title = Structural basis for activation of the titin kinase domain during myofibrillogenesis | journal = Nature | volume = 395 | issue = 6705 | pages = 863–9 | date = Oct 1998 | pmid = 9804419 | doi = 10.1038/27603 | bibcode = 1998Natur.395..863M | s2cid = 4426977 }} * {{cite journal | vauthors = Moreira ES, Wiltshire TJ, Faulkner G, Nilforoushan A, Vainzof M, Suzuki OT, Valle G, Reeves R, Zatz M, Passos-Bueno MR, Jenne DE | title = Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin | journal = Nature Genetics | volume = 24 | issue = 2 | pages = 163–6 | date = Feb 2000 | pmid = 10655062 | doi = 10.1038/72822 | s2cid = 8698402 }} * {{cite journal | vauthors = Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G | title = FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle | journal = The Journal of Biological Chemistry | volume = 275 | issue = 52 | pages = 41234–42 | date = Dec 2000 | pmid = 10984498 | doi = 10.1074/jbc.M007493200 | doi-access = free | hdl = 11368/1698365 | hdl-access = free }} * {{cite journal | vauthors = Schröder R, Reimann J, Iakovenko A, Mues A, Bönnemann CG, Matten J, Gautel M | title = Early and selective disappearance of telethonin protein from the sarcomere in neurogenic atrophy | journal = Journal of Muscle Research and Cell Motility | volume = 22 | issue = 3 | pages = 259–64 | year = 2002 | pmid = 11763198 | doi = 10.1023/A:1012242011109 | s2cid = 22553971 }} * {{cite journal | vauthors = Frey N, Olson EN | title = Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins | journal = The Journal of Biological Chemistry | volume = 277 | issue = 16 | pages = 13998–4004 | date = Apr 2002 | pmid = 11842093 | doi = 10.1074/jbc.M200712200 | doi-access = free }} * {{cite journal | vauthors = Nicholas G, Thomas M, Langley B, Somers W, Patel K, Kemp CF, Sharma M, Kambadur R | title = Titin-cap associates with, and regulates secretion of, Myostatin | journal = Journal of Cellular Physiology | volume = 193 | issue = 1 | pages = 120–31 | date = Oct 2002 | pmid = 12209887 | doi = 10.1002/jcp.10158 | s2cid = 8866409 | url = http://researchonline.rvc.ac.uk/id/eprint/1181/ | url-access = subscription }} * {{cite journal | vauthors = Zou P, Gautel M, Geerlof A, Wilmanns M, Koch MH, Svergun DI | title = Solution scattering suggests cross-linking function of telethonin in the complex with titin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 4 | pages = 2636–44 | date = Jan 2003 | pmid = 12446666 | doi = 10.1074/jbc.M210217200 | doi-access = free }} * {{cite journal | vauthors = Knöll R, Hoshijima M, Hoffman HM, Person V, Lorenzen-Schmidt I, Bang ML, Hayashi T, Shiga N, Yasukawa H, Schaper W, McKenna W, Yokoyama M, Schork NJ, Omens JH, McCulloch AD, Kimura A, Gregorio CC, Poller W, Schaper J, Schultheiss HP, Chien KR | title = The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy | journal = Cell | volume = 111 | issue = 7 | pages = 943–55 | date = Dec 2002 | pmid = 12507422 | doi = 10.1016/S0092-8674(02)01226-6 | s2cid = 15082967 | doi-access = free }} * {{cite journal | vauthors = Katoh M, Katoh M | title = Evolutionary recombination hotspot around GSDML-GSDM locus is closely linked to the oncogenomic recombination hotspot around the PPP1R1B-ERBB2-GRB7 amplicon | journal = International Journal of Oncology | volume = 24 | issue = 4 | pages = 757–63 | date = Apr 2004 | pmid = 15010812 | doi = 10.3892/ijo.24.4.757 }} * {{cite journal | vauthors = Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G | title = The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle | journal = Journal of Molecular Biology | volume = 339 | issue = 2 | pages = 313–25 | date = May 2004 | pmid = 15136035 | doi = 10.1016/j.jmb.2004.03.071 }} * {{cite journal | vauthors = Hayashi T, Arimura T, Itoh-Satoh M, Ueda K, Hohda S, Inagaki N, Takahashi M, Hori H, Yasunami M, Nishi H, Koga Y, Nakamura H, Matsuzaki M, Choi BY, Bae SW, You CW, Han KH, Park JE, Knöll R, Hoshijima M, Chien KR, Kimura A | title = Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy | journal = Journal of the American College of Cardiology | volume = 44 | issue = 11 | pages = 2192–201 | date = Dec 2004 | pmid = 15582318 | doi = 10.1016/j.jacc.2004.08.058 | doi-access = free }} {{refend}}
== External links == * [https://www.ncbi.nlm.nih.gov/books/NBK1768/ GeneReviews/NIH/NCBI/UW entry on Familial Hypertrophic Cardiomyopathy Overview]
{{PDB Gallery|geneid=8557}} {{Muscle tissue}}