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{{Infobox_gene}}
'''Myotilin''' is a [[protein]] that in humans is encoded by the ''MYOT'' [[gene]].<ref name="pmid10486214">{{cite journal |vauthors=Godley LA, Lai F, Liu J, Zhao N, Le Beau MM | title = TTID: A novel gene at 5q31 encoding a protein with titin-like features | journal = Genomics | volume = 60 | issue = 2 | pages = 226–33 |date=Nov 1999 | pmid = 10486214 | pmc =  | doi = 10.1006/geno.1999.5912 }}</ref><ref name="pmid10369880">{{cite journal |vauthors=Salmikangas P, Mykkanen OM, Gronholm M, Heiska L, Kere J, Carpen O | title = Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy | journal = Hum Mol Genet | volume = 8 | issue = 7 | pages = 1329–36 |date=Aug 1999 | pmid = 10369880 | pmc =  | doi =10.1093/hmg/8.7.1329  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MYOT myotilin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9499| accessdate = }}</ref> Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the [[sarcomere|Z-disc]] of [[sarcomere]]s.
 
== Structure ==
Myotilin is a 55.3 kDa protein composed of 496 amino acids.<ref name="url_COPaKB">{{cite web | url = http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=Q9JIF9 | work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) | title = Myotilin protein information }}</ref> Myotilin was originally identified as a novel [[ACTN2|alpha-actinin]] binding partner with two [[immunoglobulin|Ig]]-like domains, that localized to the [[sarcomere|Z-disc]].<ref>{{cite journal | vauthors = Salmikangas P, Mykkänen OM, Grönholm M, Heiska L, Kere J, Carpén O | title = Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy | journal = Human Molecular Genetics | volume = 8 | issue = 7 | date = Jul 1999 | pmid = 10369880 | doi=10.1093/hmg/8.7.1329 | pages=1329–36}}</ref> The C2-type [[immunoglobulin|Ig]]-like domains reside at the C-terminal half, and are most homologous to [[immunoglobulin|Ig]] domains 2-3 of [[palladin]] and [[immunoglobulin|Ig]] domains 4-5 of [[MYPN|myopalladin]] and more distantly related to [[sarcomere|Z-disc]] [[immunoglobulin|Ig]] domains 7 and 8 of [[titin]]. The C-terminal region hosts the binding sites for Z-band proteins, and 2 [[immunoglobulin|Ig]] domains are the site of homodimerization for myotilin.<ref name="pmid19458539">{{cite journal | vauthors = Shalaby S, Mitsuhashi H, Matsuda C, Minami N, Noguchi S, Nonaka I, Nishino I, Hayashi YK | title = Defective myotilin homodimerization caused by a novel mutation in MYOT exon 9 in the first Japanese limb girdle muscular dystrophy 1A patient | journal = Journal of Neuropathology and Experimental Neurology | volume = 68 | issue = 6 | date = Jun 2009 | pmid = 19458539 | doi = 10.1097/NEN.0b013e3181a7f703 | pages=701–7}}</ref> By contrast, the N-terminal part of myotilin is unique, consisting of a [[serine]]-rich region with no homology to known proteins. Several disease-associated mutations involve [[serine]] residues within the [[serine]]-rich domain.<ref name="pmid21256014">{{cite journal | vauthors = Selcen D | title = Myofibrillar myopathies | journal = Neuromuscular Disorders | volume = 21 | issue = 3 | date = Mar 2011 | pmid = 21256014 | doi = 10.1016/j.nmd.2010.12.007 | pages=161–71 | pmc=3052736}}</ref> Myotilin expression in human tissues is mainly restricted to striated muscles and nerves. In muscles, myotilin is predominantly found within the [[sarcomere|Z-discs]]. Myotilin forms homodimers and binds [[ACTN2|alpha-actinin]], [[ACTA1|actin]],<ref>{{cite journal | vauthors = Salmikangas P, van der Ven PF, Lalowski M, Taivainen A, Zhao F, Suila H, Schröder R, Lappalainen P, Fürst DO, Carpén O | title = Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly | journal = Human Molecular Genetics | volume = 12 | issue = 2 | date = Jan 2003 | pmid = 12499399 | doi=10.1093/hmg/ddg020 | pages=189–203}}</ref> [[FLNC|Filamin C]],<ref>{{cite journal | vauthors = van der Ven PF, Wiesner S, Salmikangas P, Auerbach D, Himmel M, Kempa S, Hayess K, Pacholsky D, Taivainen A, Schröder R, Carpén O, Fürst DO | title = Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin | journal = The Journal of Cell Biology | volume = 151 | issue = 2 | date = Oct 2000 | pmid = 11038172 | doi=10.1083/jcb.151.2.235 | pmc=2192634 | pages=235–248}}</ref> [[MYOZ1|FATZ-1]],<ref name="pmid16076904"/> [[MYOZ2|FATZ-2]] <ref name="pmid16076904">{{cite journal | vauthors = Gontier Y, Taivainen A, Fontao L, Sonnenberg A, van der Flier A, Carpen O, Faulkner G, Borradori L | title = The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins | journal = Journal of Cell Science | volume = 118 | issue = Pt 16 | date = Aug 2005 | pmid = 16076904 | doi = 10.1242/jcs.02484 | pages=3739–49}}</ref> and [[LDB3|ZASP]].<ref>{{cite journal | vauthors = von Nandelstadh P, Ismail M, Gardin C, Suila H, Zara I, Belgrano A, Valle G, Carpen O, Faulkner G | title = A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies | journal = Molecular and Cellular Biology | volume = 29 | issue = 3 | date = Feb 2009 | pmid = 19047374 | doi = 10.1128/MCB.01454-08 | pages=822–34 | pmc=2630697}}</ref>
 
==Function==
Myotilin is a structural protein that, along with [[titin]] and [[ACTN2|alpha-actinin]] give structural integrity to [[sarcomere]]s at [[sarcomere|Z-disc]]s in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells. A ternary complex myotilin/[[ACTA1|actin]]/[[ACTN2|alpha-actinin]] can be observed in vitro and [[actin]] bundles formed under these conditions appear more tightly packed than those induced by [[ACTN2|alpha-actinin]] alone. It was demonstrated that myotilin stabilizes [[F-actin]] by slowing down the disassembly rate. Ectopic overexpression of truncated myotilin causes the disruption of nascent myofibrils and the co-accumulation of myotilin and [[titin]] in amorphous cytoplasmic precipitates. In mature [[sarcomere]]s, wild-type myotilin colocalizes with [[ACTN2|alpha-actinin]] and [[sarcomere|Z-disc]] [[titin]], showing the striated pattern typical of [[sarcomere|sarcomeric]] proteins. Targeted disruption of the myotilin gene in mice does not cause significant alterations in muscle function.<ref>{{cite journal | vauthors = Moza M ''et al'' | year = 2007 | title = Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice | url = | journal = Mol Cell Biol | volume = 27 | issue = 1| pages = 244–252 | doi=10.1128/mcb.00561-06}}</ref> On the other hand, transgenic mice with mutated myotilin develop muscle dystrophy.<ref>{{cite journal | vauthors = Garvey SM ''et al'' | year = 2006 | title = Transgenic mice expressing the myotilin T57I mutation unite the pathology associated with LGMD1A and MFM | url = | journal = Hum Mol Genet | volume = 15 | issue = 15| pages = 2348–62 | doi=10.1093/hmg/ddl160 | pmid=16801328}}</ref>
 
==Clinical significance==
Myotilin is mutated in various forms of muscular dystrophy: Limb-Girdle Muscular Dystrophy type 1A (LGMD1A), Myofibrillar Myopathy (MFM), Spheroid Body Myopathy and Distal Myopath.<ref name="pmid21256014"/> The mechanism underlying the pathology is still under investigation. It has been shown that actin binding properties of myotilin housing pathogenic mutations ([[serine|Ser]]55[[phenylalanine|Phe]], [[Threonine|Thr]]57[[isoleucine|Ile]], [[serine|Ser]]60[[cysteine|Cys]], and [[serine|Ser]]95[[isoleucine|Ile]]) are normal,<ref name="pmid16122733">{{cite journal | vauthors = von Nandelstadh P, Grönholm M, Moza M, Lamberg A, Savilahti H, Carpén O | title = Actin-organising properties of the muscular dystrophy protein myotilin | journal = Experimental Cell Research | volume = 310 | issue = 1 | date = Oct 2005 | pmid = 16122733 | doi = 10.1016/j.yexcr.2005.06.027 | pages=131–9}}</ref> albeit with a slower rate of degradation.<ref name="pmid21361873">{{cite journal | vauthors = von Nandelstadh P, Soliymani R, Baumann M, Carpen O | title = Analysis of myotilin turnover provides mechanistic insight into the role of myotilinopathy-causing mutations | journal = The Biochemical Journal | volume = 436 | issue = 1 | date = May 2011 | pmid = 21361873 | doi = 10.1042/BJ20101672 | pages=113–21}}</ref> Surprisingly, YFP-fusion constructs of myotilin mutants ([[serine|Ser]]55[[phenylalanine|Phe]], [[serine|Ser]]55[[isoleucine|Ile]], [[Threonine|Thr]]57[[isoleucine|Ile]], [[serine|Ser]]60[[cysteine|Cys]], [[serine|Ser]]60[[phenylalanine|Phe]], [[serine|Ser]]95[[isoleucine|Ile]], [[arginine|Arg]]405[[lysine|Lys]]) localized normally to [[sarcomere|Z-discs]] and exhibited normal dynamics in muscle cells.<ref name="pmid22021208">{{cite journal | vauthors = Wang J, Dube DK, Mittal B, Sanger JM, Sanger JW | title = Myotilin dynamics in cardiac and skeletal muscle cells | journal = Cytoskeleton | volume = 68 | issue = 12 | date = Dec 2011 | pmid = 22021208 | doi = 10.1002/cm.20542 | pages=661–70 | pmc=3240742}}</ref>
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Speer MC, Yamaoka LH, Gilchrist JH, Gaskell CP, Stajich JM, Vance JM, Kazantsev A, Lastra AA, Haynes CS, Beckmann JS | title = Confirmation of genetic heterogeneity in limb-girdle muscular dystrophy: linkage of an autosomal dominant form to chromosome 5q | journal = American Journal of Human Genetics | volume = 50 | issue = 6 | pages = 1211–7 | date = Jun 1992 | pmid = 1598902 | pmc = 1682558 | doi =  }}
* {{cite journal | vauthors = Dixon MJ, Read AP, Donnai D, Colley A, Dixon J, Williamson R | title = The gene for Treacher Collins syndrome maps to the long arm of chromosome 5 | journal = American Journal of Human Genetics | volume = 49 | issue = 1 | pages = 17–22 | date = Jul 1991 | pmid = 1676560 | pmc = 1683211 | doi =  }}
* {{cite journal | vauthors = Bartoloni L, Horrigan SK, Viles KD, Gilchrist JM, Stajich JM, Vance JM, Yamaoka LH, Pericak-Vance MA, Westbrook CA, Speer MC | title = Use of a CEPH meiotic breakpoint panel to refine the locus of limb-girdle muscular dystrophy type 1A (LGMD1A) to a 2-Mb interval on 5q31 | journal = Genomics | volume = 54 | issue = 2 | pages = 250–5 | date = Dec 1998 | pmid = 9828127 | doi = 10.1006/geno.1998.5579 }}
* {{cite journal | vauthors = Hauser MA, Horrigan SK, Salmikangas P, Torian UM, Viles KD, Dancel R, Tim RW, Taivainen A, Bartoloni L, Gilchrist JM, Stajich JM, Gaskell PC, Gilbert JR, Vance JM, Pericak-Vance MA, Carpen O, Westbrook CA, Speer MC | title = Myotilin is mutated in limb girdle muscular dystrophy 1A | journal = Human Molecular Genetics | volume = 9 | issue = 14 | pages = 2141–7 | date = Sep 2000 | pmid = 10958653 | doi = 10.1093/hmg/9.14.2141 }}
* {{cite journal | vauthors = van der Ven PF, Wiesner S, Salmikangas P, Auerbach D, Himmel M, Kempa S, Hayess K, Pacholsky D, Taivainen A, Schröder R, Carpén O, Fürst DO | title = Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin | journal = The Journal of Cell Biology | volume = 151 | issue = 2 | pages = 235–48 | date = Oct 2000 | pmid = 11038172 | pmc = 2192634 | doi = 10.1083/jcb.151.2.235 }}
* {{cite journal | vauthors = Hauser MA, Conde CB, Kowaljow V, Zeppa G, Taratuto AL, Torian UM, Vance J, Pericak-Vance MA, Speer MC, Rosa AL | title = myotilin Mutation found in second pedigree with LGMD1A | journal = American Journal of Human Genetics | volume = 71 | issue = 6 | pages = 1428–32 | date = Dec 2002 | pmid = 12428213 | pmc = 378586 | doi = 10.1086/344532 }}
* {{cite journal | vauthors = Salmikangas P, van der Ven PF, Lalowski M, Taivainen A, Zhao F, Suila H, Schröder R, Lappalainen P, Fürst DO, Carpén O | title = Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly | journal = Human Molecular Genetics | volume = 12 | issue = 2 | pages = 189–203 | date = Jan 2003 | pmid = 12499399 | doi = 10.1093/hmg/ddg020 }}
* {{cite journal | vauthors = Battle MA, Maher VM, McCormick JJ | title = ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways | journal = Biochemistry | volume = 42 | issue = 24 | pages = 7270–82 | date = Jun 2003 | pmid = 12809483 | doi = 10.1021/bi034081y }}
* {{cite journal | vauthors = Selcen D, Engel AG | title = Mutations in myotilin cause myofibrillar myopathy | journal = Neurology | volume = 62 | issue = 8 | pages = 1363–71 | date = Apr 2004 | pmid = 15111675 | doi = 10.1212/01.wnl.0000123576.74801.75 }}
* {{cite journal | vauthors = Witt SH, Granzier H, Witt CC, Labeit S | title = MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination | journal = Journal of Molecular Biology | volume = 350 | issue = 4 | pages = 713–22 | date = Jul 2005 | pmid = 15967462 | doi = 10.1016/j.jmb.2005.05.021 }}
* {{cite journal | vauthors = Gontier Y, Taivainen A, Fontao L, Sonnenberg A, van der Flier A, Carpen O, Faulkner G, Borradori L | title = The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins | journal = Journal of Cell Science | volume = 118 | issue = Pt 16 | pages = 3739–49 | date = Aug 2005 | pmid = 16076904 | doi = 10.1242/jcs.02484 }}
* {{cite journal | vauthors = von Nandelstadh P, Grönholm M, Moza M, Lamberg A, Savilahti H, Carpén O | title = Actin-organising properties of the muscular dystrophy protein myotilin | journal = Experimental Cell Research | volume = 310 | issue = 1 | pages = 131–9 | date = Oct 2005 | pmid = 16122733 | doi = 10.1016/j.yexcr.2005.06.027 }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
* {{cite journal | vauthors = Foroud T, Pankratz N, Batchman AP, Pauciulo MW, Vidal R, Miravalle L, Goebel HH, Cushman LJ, Azzarelli B, Horak H, Farlow M, Nichols WC | title = A mutation in myotilin causes spheroid body myopathy | journal = Neurology | volume = 65 | issue = 12 | pages = 1936–40 | date = Dec 2005 | pmid = 16380616 | doi = 10.1212/01.wnl.0000188872.28149.9a }}
* {{cite journal | vauthors = Garvey SM, Senderek J, Beckmann JS, Seboun E, Jackson CE, Hauser MA | title = Myotilin is not the causative gene for vocal cord and pharyngeal weakness with distal myopathy (VCPDM) | journal = Annals of Human Genetics | volume = 70 | issue = Pt 3 | pages = 414–6 | date = May 2006 | pmid = 16674563 | doi = 10.1111/j.1529-8817.2005.00252.x }}
* {{cite journal | vauthors = Pénisson-Besnier I, Talvinen K, Dumez C, Vihola A, Dubas F, Fardeau M, Hackman P, Carpen O, Udd B | title = Myotilinopathy in a family with late onset myopathy | journal = Neuromuscular Disorders | volume = 16 | issue = 7 | pages = 427–31 | date = Jul 2006 | pmid = 16793270 | doi = 10.1016/j.nmd.2006.04.009 }}
{{refend}}
 
==External links==
* {{cite journal | doi =  10.1161/CIRCRESAHA.113.301151 |  PMID = 23965338 | pmc=4076475 | volume=113 | title=Integration of cardiac proteome biology and medicine by a specialized knowledgebase. | date=Oct 2013 | journal=Circ Res | pages=1043–53 | vauthors=Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P}}
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=mfm  GeneReviews/NIH/NCBI/UW entry on Myofibrillar Myopathy]
 
{{Muscle tissue}}
 
[[Category:Human proteins]]

Revision as of 07:15, 4 September 2017

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Myotilin is a protein that in humans is encoded by the MYOT gene.[1][2][3] Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres.

Structure

Myotilin is a 55.3 kDa protein composed of 496 amino acids.[4] Myotilin was originally identified as a novel alpha-actinin binding partner with two Ig-like domains, that localized to the Z-disc.[5] The C2-type Ig-like domains reside at the C-terminal half, and are most homologous to Ig domains 2-3 of palladin and Ig domains 4-5 of myopalladin and more distantly related to Z-disc Ig domains 7 and 8 of titin. The C-terminal region hosts the binding sites for Z-band proteins, and 2 Ig domains are the site of homodimerization for myotilin.[6] By contrast, the N-terminal part of myotilin is unique, consisting of a serine-rich region with no homology to known proteins. Several disease-associated mutations involve serine residues within the serine-rich domain.[7] Myotilin expression in human tissues is mainly restricted to striated muscles and nerves. In muscles, myotilin is predominantly found within the Z-discs. Myotilin forms homodimers and binds alpha-actinin, actin,[8] Filamin C,[9] FATZ-1,[10] FATZ-2 [10] and ZASP.[11]

Function

Myotilin is a structural protein that, along with titin and alpha-actinin give structural integrity to sarcomeres at Z-discs in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells. A ternary complex myotilin/actin/alpha-actinin can be observed in vitro and actin bundles formed under these conditions appear more tightly packed than those induced by alpha-actinin alone. It was demonstrated that myotilin stabilizes F-actin by slowing down the disassembly rate. Ectopic overexpression of truncated myotilin causes the disruption of nascent myofibrils and the co-accumulation of myotilin and titin in amorphous cytoplasmic precipitates. In mature sarcomeres, wild-type myotilin colocalizes with alpha-actinin and Z-disc titin, showing the striated pattern typical of sarcomeric proteins. Targeted disruption of the myotilin gene in mice does not cause significant alterations in muscle function.[12] On the other hand, transgenic mice with mutated myotilin develop muscle dystrophy.[13]

Clinical significance

Myotilin is mutated in various forms of muscular dystrophy: Limb-Girdle Muscular Dystrophy type 1A (LGMD1A), Myofibrillar Myopathy (MFM), Spheroid Body Myopathy and Distal Myopath.[7] The mechanism underlying the pathology is still under investigation. It has been shown that actin binding properties of myotilin housing pathogenic mutations (Ser55Phe, Thr57Ile, Ser60Cys, and Ser95Ile) are normal,[14] albeit with a slower rate of degradation.[15] Surprisingly, YFP-fusion constructs of myotilin mutants (Ser55Phe, Ser55Ile, Thr57Ile, Ser60Cys, Ser60Phe, Ser95Ile, Arg405Lys) localized normally to Z-discs and exhibited normal dynamics in muscle cells.[16]

References

  1. ↑ Godley LA, Lai F, Liu J, Zhao N, Le Beau MM (Nov 1999). "TTID: A novel gene at 5q31 encoding a protein with titin-like features". Genomics. 60 (2): 226–33. doi:10.1006/geno.1999.5912. PMID 10486214.
  2. ↑ Salmikangas P, Mykkanen OM, Gronholm M, Heiska L, Kere J, Carpen O (Aug 1999). "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy". Hum Mol Genet. 8 (7): 1329–36. doi:10.1093/hmg/8.7.1329. PMID 10369880.
  3. ↑ "Entrez Gene: MYOT myotilin".
  4. ↑ "Myotilin protein information". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).
  5. ↑ Salmikangas P, Mykkänen OM, Grönholm M, Heiska L, Kere J, Carpén O (Jul 1999). "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy". Human Molecular Genetics. 8 (7): 1329–36. doi:10.1093/hmg/8.7.1329. PMID 10369880.
  6. ↑ Shalaby S, Mitsuhashi H, Matsuda C, Minami N, Noguchi S, Nonaka I, Nishino I, Hayashi YK (Jun 2009). "Defective myotilin homodimerization caused by a novel mutation in MYOT exon 9 in the first Japanese limb girdle muscular dystrophy 1A patient". Journal of Neuropathology and Experimental Neurology. 68 (6): 701–7. doi:10.1097/NEN.0b013e3181a7f703. PMID 19458539.
  7. ↑ 7.0 7.1 Selcen D (Mar 2011). "Myofibrillar myopathies". Neuromuscular Disorders. 21 (3): 161–71. doi:10.1016/j.nmd.2010.12.007. PMC 3052736. PMID 21256014.
  8. ↑ Salmikangas P, van der Ven PF, Lalowski M, Taivainen A, Zhao F, Suila H, Schröder R, Lappalainen P, Fürst DO, Carpén O (Jan 2003). "Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly". Human Molecular Genetics. 12 (2): 189–203. doi:10.1093/hmg/ddg020. PMID 12499399.
  9. ↑ van der Ven PF, Wiesner S, Salmikangas P, Auerbach D, Himmel M, Kempa S, Hayess K, Pacholsky D, Taivainen A, Schröder R, Carpén O, Fürst DO (Oct 2000). "Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin". The Journal of Cell Biology. 151 (2): 235–248. doi:10.1083/jcb.151.2.235. PMC 2192634. PMID 11038172.
  10. ↑ 10.0 10.1 Gontier Y, Taivainen A, Fontao L, Sonnenberg A, van der Flier A, Carpen O, Faulkner G, Borradori L (Aug 2005). "The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins". Journal of Cell Science. 118 (Pt 16): 3739–49. doi:10.1242/jcs.02484. PMID 16076904.
  11. ↑ von Nandelstadh P, Ismail M, Gardin C, Suila H, Zara I, Belgrano A, Valle G, Carpen O, Faulkner G (Feb 2009). "A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies". Molecular and Cellular Biology. 29 (3): 822–34. doi:10.1128/MCB.01454-08. PMC 2630697. PMID 19047374.
  12. ↑ Moza M, et al. (2007). "Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice". Mol Cell Biol. 27 (1): 244–252. doi:10.1128/mcb.00561-06.
  13. ↑ Garvey SM, et al. (2006). "Transgenic mice expressing the myotilin T57I mutation unite the pathology associated with LGMD1A and MFM". Hum Mol Genet. 15 (15): 2348–62. doi:10.1093/hmg/ddl160. PMID 16801328.
  14. ↑ von Nandelstadh P, Grönholm M, Moza M, Lamberg A, Savilahti H, Carpén O (Oct 2005). "Actin-organising properties of the muscular dystrophy protein myotilin". Experimental Cell Research. 310 (1): 131–9. doi:10.1016/j.yexcr.2005.06.027. PMID 16122733.
  15. ↑ von Nandelstadh P, Soliymani R, Baumann M, Carpen O (May 2011). "Analysis of myotilin turnover provides mechanistic insight into the role of myotilinopathy-causing mutations". The Biochemical Journal. 436 (1): 113–21. doi:10.1042/BJ20101672. PMID 21361873.
  16. ↑ Wang J, Dube DK, Mittal B, Sanger JM, Sanger JW (Dec 2011). "Myotilin dynamics in cardiac and skeletal muscle cells". Cytoskeleton. 68 (12): 661–70. doi:10.1002/cm.20542. PMC 3240742. PMID 22021208.

Further reading

  • Speer MC, Yamaoka LH, Gilchrist JH, Gaskell CP, Stajich JM, Vance JM, Kazantsev A, Lastra AA, Haynes CS, Beckmann JS (Jun 1992). "Confirmation of genetic heterogeneity in limb-girdle muscular dystrophy: linkage of an autosomal dominant form to chromosome 5q". American Journal of Human Genetics. 50 (6): 1211–7. PMC 1682558. PMID 1598902.
  • Dixon MJ, Read AP, Donnai D, Colley A, Dixon J, Williamson R (Jul 1991). "The gene for Treacher Collins syndrome maps to the long arm of chromosome 5". American Journal of Human Genetics. 49 (1): 17–22. PMC 1683211. PMID 1676560.
  • Bartoloni L, Horrigan SK, Viles KD, Gilchrist JM, Stajich JM, Vance JM, Yamaoka LH, Pericak-Vance MA, Westbrook CA, Speer MC (Dec 1998). "Use of a CEPH meiotic breakpoint panel to refine the locus of limb-girdle muscular dystrophy type 1A (LGMD1A) to a 2-Mb interval on 5q31". Genomics. 54 (2): 250–5. doi:10.1006/geno.1998.5579. PMID 9828127.
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External links

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