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{{Short description|Protein encoded by the DYSF gene in humans}}
{{Infobox_gene}}
'''Dysferlin''' also known as '''dystrophy-associated fer-1-like protein''' is a [[protein]] that in humans is encoded by the ''DYSF'' [[gene]].<ref name="pmid8320700">{{cite journal |vauthors=Passos-Bueno MR, Richard I, Vainzof M, Fougerousse F, Weissenbach J, Broux O, Cohen D, Akiyama J, Marie SK, Carvalho AA |title=Evidence of genetic heterogeneity in the autosomal recessive adult forms of limb-girdle muscular dystrophy following linkage analysis with 15q probes in Brazilian families |journal=[[Journal of Medical Genetics]]| volume=30 |issue=5 |pages=385–7 |date=May 1993 |pmid=8320700 |pmc=1016373 |doi=10.1136/jmg.30.5.385 }}</ref> Dysferlin is linked with plasma membrane repair.,<ref name="entrez">{{cite web |title=Entrez Gene: DYSF dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)| url=https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8291}}</ref> stabilization of calcium signaling<ref>{{cite journal |vauthors=Kerr JP, Ziman AP, Mueller AL, Muriel JM, Kleinhans-Welte E, Gumerson JD, Vogel SS, Ward CW, Roche JA, Bloch RJ |display-authors=3 |title=Dysferlin Stabilizes Stress-induced Ca2+ Signaling in the Transverse Tubule Membrane |journal=Proc. Natl. Acad. Sci. USA |volume=110 |pages=20831–20836 |date=December 2013 |issue=51 |pmid=24302765 |doi=10.1073/pnas.1307960110 |pmc=3870721|bibcode=2013PNAS..11020831K |doi-access=free }}</ref><ref>{{cite journal |vauthors=Kerr JP, Ward CW, Bloch RJ| title=Dysferlin at Transverse Tubules Regulates Ca2+ Homeostasis in Skeletal Muscle |journal=Frontiers in Physiology |volume=5 | pages=89 |date=March 2014 |pmid=24639655 |doi=10.3389/fphys.2014.00089 |pmc=3944681| doi-access=free }}</ref><ref>{{cite journal |vauthors=Lukyanenko V, Muriel JM, Bloch RJ| title=Coupling of Excitation to Ca2+ Release is Modulated by Dysferlin |journal=J. Physiol. |volume=595 |pages=5191–5207 |date=August 2017 | issue=15 |pmid=8568606 |doi=10.1113/JP274515 |pmc=5538227}}</ref> and the development of the T-tubule system of the muscle<ref>{{cite journal |vauthors=Hofhuis J, Bersch K, Wagner S, Molina C, Fakuade FE, Iyer LM, Streckfuss-Bömeke K, Toischer K, Zelarayán LC, Voigt N, Nikolaev VO, Maier LS, Klinge L, Thoms S| title=Dysferlin links excitation-contraction coupling to structure and maintenance of the cardiac transverse-axial tubule system |journal=Europace |volume=22 |pages=1119–1131 |date=July 2020 | issue=7 |pmid=32572487 |doi=10.1093/europace/euaa093|doi-access=free }}</ref> A defect in the DYSF gene, located on [[chromosome 2]]p12-14, results in several types of [[muscular dystrophy]]; including [[Miyoshi myopathy]] (MM), [[Limb-girdle muscular dystrophy]] type 2B (LGMD2B) and Distal Myopathy (DM). A reduction or absence of dysferlin, termed [[dysferlinopathy]], usually becomes apparent in the third or fourth decade of life and is characterised by weakness and wasting of various voluntary [[skeletal muscles]].<ref>[http://www.dmd.nl/dysf_home.html#disease Leiden University Medical Center, Center for Human and Clinical Genetics - Dysferlin] Retrieved 21 June 2007.</ref> Pathogenic mutations leading to dysferlinopathy can occur throughout the DYSF gene.
== Structure ==
{{Infobox protein family |Symbol = Dysferlin |Name = Ferlin family |align=left |Pfam = |InterPro = |SMART = |SCOP = |PDB = |OPM family = 452 |OPM protein=4cah |Membranome superfamily = 205}}
The human dysferlin protein is a 237 kilodalton type-II transmembrane protein.<ref>{{cite journal | vauthors = Kawahara G, Serafini PR, Myers JA, Alexander MS, Kunkel LM | title = Characterization of zebrafish dysferlin by morpholino knockdown | journal = Biochemical and Biophysical Research Communications | volume = 413 | issue = 2 | pages = 358–363 | date = September 2011 | pmid = 21893049 | pmc = 4526276 | doi = 10.1016/j.bbrc.2011.08.105 }}</ref><ref name=":0">{{cite journal | vauthors = Fuson K, Rice A, Mahling R, Snow A, Nayak K, Shanbhogue P, Meyer AG, Redpath GM, Hinderliter A, Cooper ST, Sutton RB | display-authors = 6 | title = Alternate splicing of dysferlin C2A confers Ca²⁺-dependent and Ca²⁺-independent binding for membrane repair | journal = Structure | volume = 22 | issue = 1 | pages = 104–115 | date = January 2014 | pmid = 24239457 | pmc = 5993433 | doi = 10.1016/j.str.2013.10.001 }}</ref><ref>{{cite journal | vauthors = Demonbreun AR, Allen MV, Warner JL, Barefield DY, Krishnan S, Swanson KE, Earley JU, McNally EM | display-authors = 6 | title = Enhanced Muscular Dystrophy from Loss of Dysferlin Is Accompanied by Impaired Annexin A6 Translocation after Sarcolemmal Disruption | journal = The American Journal of Pathology | volume = 186 | issue = 6 | pages = 1610–1622 | date = June 2016 | pmid = 27070822 | pmc = 4901136 | doi = 10.1016/j.ajpath.2016.02.005 }}</ref><ref>{{cite journal | vauthors = Cacciottolo M, Numitone G, Aurino S, Caserta IR, Fanin M, Politano L, Minetti C, Ricci E, Piluso G, Angelini C, Nigro V | display-authors = 6 | title = Muscular dystrophy with marked Dysferlin deficiency is consistently caused by primary dysferlin gene mutations | journal = European Journal of Human Genetics | volume = 19 | issue = 9 | pages = 974–980 | date = September 2011 | pmid = 21522182 | pmc = 3179367 | doi = 10.1038/ejhg.2011.70 }}</ref><ref>{{cite journal | vauthors = Matsuda C, Kiyosue K, Nishino I, Goto Y, Hayashi YK | title = Dysferlinopathy Fibroblasts Are Defective in Plasma Membrane Repair | journal = PLOS Currents | volume = 7 | date = October 2015 | pmid = 26579332 | pmc = 4639325 | doi = 10.1371/currents.md.5865add2d766f39a0e0411d38a7ba09c | doi-access = free }}</ref> It contains a large intracellular cytoplasmic N-terminal ___domain, an extreme C-terminal transmembrane ___domain, and a short C-terminal extracellular ___domain. The cytosolic ___domain of dysferlin is composed of seven highly conserved [[C2 domains]] (C2A-G) which are conserved across several proteins within the [[ferlin family]], including dysferlin homolog [[myoferlin]].<ref name="pmid11234777">{{cite journal | vauthors = Vafiadaki E, Reis A, Keers S, Harrison R, Anderson LV, Raffelsberger T, Ivanova S, Hoger H, Bittner RE, Bushby K, Bashir R | display-authors = 6 | title = Cloning of the mouse dysferlin gene and genomic characterization of the SJL-Dysf mutation | journal = NeuroReport | volume = 12 | issue = 3 | pages = 625–629 | date = March 2001 | pmid = 11234777 | doi = 10.1097/00001756-200103050-00039 | s2cid = 22800606 }}</ref><ref>{{cite journal | vauthors = Abdullah N, Padmanarayana M, Marty NJ, Johnson CP | title = Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin | journal = Biophysical Journal | volume = 106 | issue = 2 | pages = 382–389 | date = January 2014 | pmid = 24461013 | pmc = 3907215 | doi = 10.1016/j.bpj.2013.11.4492 | bibcode = 2014BpJ...106..382A }}</ref><ref name=":0" /> In fact, the C2 ___domain at any given position is more similar to the C2 ___domain at the corresponding position within other ferlin family members than the adjacent C2 ___domain within the same protein. This suggests that each individual C2 ___domain may in fact play a specific role in dysferlin function and each has in fact been shown to be required for two of dysferlin's roles stabilization of calcium signaling and membrane repair.<ref>{{cite journal | vauthors = Muriel J, Lukyanenko V, Kwiatkowski T, Bhattacharya S, Garman D, Weisleder N, Bloch RJ | title = The C2 domains of dysferlin: roles in membrane localization, Ca<sup>2+</sup> signalling and sarcolemmal repair | journal = The Journal of Physiology | volume = 600 | issue = 8 | pages = 1953–1968 | date = April 2022 | pmid = 35156706 | pmc = 9285653 | doi = 10.1113/JP282648 }}</ref> Mutations in each of these domains can cause dysferlinopathy. A crystal structure of the C2A ___domain of human dysferlin has been solved, and reveals that the C2A ___domain changes conformation when interacting with calcium ions,<ref name=":0" /> which is consistent with a growing body of evidence suggesting that the C2A ___domain plays a role in calcium-dependent lipid binding.<ref name="pmid19253956">{{cite journal | vauthors = Therrien C, Di Fulvio S, Pickles S, Sinnreich M | title = Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides | journal = Biochemistry | volume = 48 | issue = 11 | pages = 2377–2384 | date = March 2009 | pmid = 19253956 | doi = 10.1021/bi802242r }}</ref> Its ability to stabilize calcium signaling in the intact dysferlin protein depends on its calcium binding activity.<ref>{{cite journal | vauthors = Lukyanenko V, Muriel J, Garman D, Breydo L, Bloch RJ | title = Elevated Ca<sup>2+</sup> at the triad junction underlies dysregulation of Ca<sup>2+</sup> signaling in dysferlin-null skeletal muscle | journal = Frontiers in Physiology | volume = 13 | pages = 1032447 | date = November 2022 | pmid = 36406982 | pmc = 9669649 | doi = 10.3389/fphys.2022.1032447 | doi-access = free }}</ref> In addition to the C2 domains, dysferlin also contains "FerA" and "DysF" domains. Mutations in both FerA<ref name=":1">{{cite journal | vauthors = Harsini FM, Chebrolu S, Fuson KL, White MA, Rice AM, Sutton RB | title = FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins | journal = Scientific Reports | volume = 8 | issue = 1 | pages = 10949 | date = July 2018 | pmid = 30026467 | pmc = 6053371 | doi = 10.1038/s41598-018-29184-1 | bibcode = 2018NatSR...810949H }}</ref> and DysF<ref name=":2">{{cite journal | vauthors = Sula A, Cole AR, Yeats C, Orengo C, Keep NH | title = Crystal structures of the human Dysferlin inner DysF ___domain | journal = BMC Structural Biology | volume = 14 | pages = 3 | date = January 2014 | pmid = 24438169 | pmc = 3898210 | doi = 10.1186/1472-6807-14-3 | doi-access = free }}</ref> can cause muscular dystrophies. DysF ___domain has an interesting structure as in contains one DysF ___domain within another DysF ___domain, a result of gene duplication; however, the function of this ___domain is currently unknown.<ref name=":2" /> FerA ___domain is conserved among all members of ferlin protein family. FerA ___domain is a four helix bundle and it can interact with membrane, usually in a calcium-dependent manner.<ref name=":1" />
== Function ==
The most intensively studied role for dysferlin is in a cellular process called membrane repair. Membrane repair is a critical mechanism by which cells are able to seal dramatic wounds to the plasma membrane. Muscle is thought to be particularly prone to membrane wounds given that muscle cells transmit high force and undergo cycles of contraction. Dysferlin is highly expressed in muscle, and is homologous to the ferlin family of proteins, which are thought to regulate membrane fusion across a wide variety of species and cell types.<ref name="pmid9731527">{{cite journal |vauthors=Bashir R, Britton S, Strachan T, Keers S, Vafiadaki E, Lako M, Richard I, Marchand S, Bourg N, Argov Z, Sadeh M, Mahjneh I, Marconi G, Passos-Bueno MR, Moreira Ede S, Zatz M, Beckmann JS, Bushby K |title=A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B |journal=Nat. Genet. |volume=20 |issue=1 |pages=37–42 |year=1998 |pmid=9731527 |doi=10.1038/1689 |s2cid=24234676}}</ref> Several lines of evidence suggest that dysferlin may be involved in membrane repair in muscle. First, dysferlin-deficient muscle fibers show accumulation of vesicles (which are critical for membrane repair in non-muscle cell types) near membrane lesions, indicating that dysferlin may be required for fusion of repair vesicles with the plasma membrane. Further, dysferlin-deficient muscle fibers take up extracellular dyes to a greater extent than wild-type muscle fibers following laser-induced wounding in-vitro.<ref name="pmid12736685">{{cite journal |vauthors=Bansal D, Miyake K, Vogel SS, Groh S, Chen CC, Williamson R, McNeil PL, Campbell KP |title=Defective membrane repair in dysferlin-deficient muscular dystrophy |journal=Nature |volume=423 |issue=6936 |pages=168–72 |year=2003 |pmid=12736685 |doi=10.1038/nature01573 |bibcode=2003Natur.423..168B |s2cid=4402938}}</ref> Dysferlin is also markedly enriched at membrane lesions with several additional proteins thought to be involved in membrane resealing, including [[annexin]] and MG53.<ref name="pmid22421042">{{cite journal |vauthors=Roostalu U, Strähle U |title=In vivo imaging of molecular interactions at damaged sarcolemma |journal=Dev. Cell |volume=22 |issue=3 |pages=515–29 |year=2012 |pmid=22421042 |doi=10.1016/j.devcel.2011.12.008 |doi-access=free}}</ref> Exactly how dysferlin contributes to membrane resealing is not clear, but biochemical evidence indicates that dysferlin may bind lipids in a calcium-dependent manner, consistent with a role for dysferlin in regulating fusion of repair vesicles with the sarcolemma during membrane repair.<ref name="pmid24461013">{{cite journal |vauthors=Abdullah N, Padmanarayana M, Marty NJ, Johnson CP |title=Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin |journal=Biophys. J. |volume=106 |issue=2 |pages=382–9 |year=2014 |pmid=24461013 |doi=10.1016/j.bpj.2013.11.4492 |pmc=3907215| bibcode=2014BpJ...106..382A}}</ref> Furthermore, live-cell imaging of dysferlin-eGFP expressing myotubes indicates that dysferlin localizes to a cellular compartment that responds to injury by forming large dysferlin-containing vesicles, and formation of these vesicles may contribute to wound repair.<ref name="pmid24203699">{{cite journal |vauthors=McDade JR, Michele DE |title=Membrane damage-induced vesicle-vesicle fusion of dysferlin-containing vesicles in muscle cells requires microtubules and kinesin |journal=Hum. Mol. Genet. |volume=23 |issue=7 |pages=1677–86 |year=2014 |pmid=24203699 |doi=10.1093/hmg/ddt557 |pmc=3943514}}</ref> Dysferlin may also be involved in Alzheimer's disease pathogenesis.<ref>{{cite journal |vauthors=Chen JA, Wang Q, Davis-Turak J, Li Y, Karydas AM, Hsu SC, Sears RL, Chatzopoulou D, Huang AY, Wojta KJ, Klein E |display-authors=3 |title=A multiancestral genome-wide exome array study of Alzheimer disease, frontotemporal dementia, and progressive supranuclear palsy |journal=JAMA Neurology |volume=72 |issue=4 |pages=414–22 |date=April 2015 |pmid=25706306 |doi=10.1001/jamaneurol.2014.4040 |pmc=4397175}}</ref>
Another well studied role for dysferlin is in stabilization of calcium signaling, especially following a mild injury. This approach was based on two observations: that muscle lacking dysferlin that is injured by eccentric contractions can repair its plasma membrane, or sarcolemma, as efficiently as healthy muscle can,<ref>{{cite journal |vauthors=Roche JA, Lovering RM, Vanapalli R, Reed PW, Bloch RJ| display-authors=3 |title=Extensive Mononuclear Infiltration and Myogenesis Characterize the Recovery of Dysferlin-Null Skeletal Muscle from Contraction-Induced Injuries. |journal=Am. J. Physiol. Cell Physiol. |volume=298 |pages=C298–C312 |date=Feb 2010 | issue=2 |pmid=9923419| doi=10.1152/ajpcell.00122.2009 |pmc=2822489}}</ref> and that most of the dysferlin in healthy muscle is concentrated in the transverse tubules at triad junctions,<ref>{{cite journal |vauthors=Kerr JP, Ziman AP, Mueller AL, Muriel JM, Kleinhans-Welte E, Gumerson JD, Vogel SS, Ward CW, Roche JA, Bloch RJ| display-authors=3 |title=Dysferlin Stabilizes Stress-induced Ca2+ Signaling in the Transverse Tubule Membrane |journal=Proc. Natl. Acad. Sci. USA |volume=110 |pages=20831–20836 |date=December 2013 | issue=51 |pmid=24302765 |doi=10.1073/pnas.1307960110 |pmc=3870721| bibcode=2013PNAS..11020831K | doi-access=free }}</ref><ref>{{cite journal |vauthors=Roche JA, Lovering RM, Vanapalli R, Reed PW, Bloch RJ| display-authors=3 |title=Extensive Mononuclear Infiltration and Myogenesis Characterize the Recovery of Dysferlin-Null Skeletal Muscle from Contraction-Induced Injuries |journal=Am. J. Physiol. Cell Physiol. |volume=298 |pages=C298–C312 |date=Feb 2010 | issue=2 |pmid=9923419| doi=10.1152/ajpcell.00122.2009 |pmc=2822489}}</ref> where calcium release is regulated. Destabilization of signaling in dysferlinopathic muscle can result in the generation of calcium waves,<ref>{{cite journal |vauthors=Lukyanenko V, Muriel J, Bloch RJ| title=Coupling of Excitation to Ca2+ Release is Modulated by Dysferlin. |journal=J. Physiol. |volume=595 |pages=5191–5207 |date=August 2017 | issue=15 |pmid=8568606 |doi=10.1113/JP274515 |pmc=5538227}}</ref> which can contribute to the disease pathology. Nearly every change in dysferlin that affects membrane repair also destabilizes calcium signaling,<ref>{{cite journal |vauthors=Muriel J, Lukyanenko V, Kwiatkowski T, Battacharya S, Garman D, Weisleder N, Bloch RJ| display-authors=3 |title=The C2 Domains of Dysferlin: Roles in Membrane Localization, Stabilization of Ca2+ Signaling, and Membrane Repair. |journal=J. Physiol. |volume=600 |pages=1953–1968 |date=Apr 2022 | issue=8 |pmid=35156706 |doi=10.1113/JP282648 |pmc=9285653}}</ref> suggesting that these two activities are closely linked. Remarkably, however, membrane repair requires calcium ions, whereas calcium ions contribute to the destabilization of signaling when dysferlin is absent or mutated.<ref>{{cite journal |vauthors=Muriel J, Lukyanenko V, Kwiatkowski T, Battacharya S, Garman D, Weisleder N, Bloch RJ |display-authors=3 |title=The C2 Domains of Dysferlin: Roles in Membrane Localization, Stabilization of Ca2+ Signaling, and Membrane Repair. |journal=J. Physiol. |volume=600 |pages=1953–1968 |date=Apr 2022 |issue=8 |pmid=35156706 |doi=10.1113/JP282648 |pmc=9285653}}</ref> These paradoxical results have yet to be reconciled.
== Interactions ==
Dysferlin has been shown to bind to itself, to form dimers and perhaps larger oligomers.<ref>{{cite journal |vauthors=Roche JA, Ru L, ONeill A, Lovering RM, Bloch RJ| display-authors=3 |title= Unmasking Potential Intracellular Roles for Dysferlin through Improved Immunolabeling Methods|journal= Journal of Histochemistry & Cytochemistry|volume=59 |pages=964–975 |date=Nov 2011 | issue=11 |pmid=22043020| doi=10.1369/0022155411423274 |pmc=3261626}}</ref> It can also has been shown to [[Protein-protein interaction|interact]] with [[Caveolin 3]] in skeletal muscle,<ref name="pmid11532985">{{cite journal |vauthors=Matsuda C, Hayashi YK, Ogawa M, Aoki M, Murayama K, Nishino I, Nonaka I, Arahata K, Brown RH |title=The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle |journal=Hum. Mol. Genet. |volume=10 |issue=17 |pages=1761–6 |date=August 2001 |pmid=11532985 |doi=10.1093/hmg/10.17.1761 |doi-access=free}}</ref> and this interaction is thought to retain dysferlin within the plasma membrane.<ref name="pmid18096699">{{cite journal |vauthors=Hernández-Deviez DJ, Howes MT, Laval SH, Bushby K, Hancock JF, Parton RG |title=Caveolin regulates endocytosis of the muscle repair protein, dysferlin |journal=J. Biol. Chem. |volume=283 |issue=10 |pages=6476–88 |year=2008 |pmid=18096699 |doi=10.1074/jbc.M708776200 |s2cid=8337318 |url=http://espace.library.uq.edu.au/view/UQ:165025/UQ165025_OA.pdf |doi-access=free}}</ref> Dysferlin also interacts with MG53, and a functional interaction between dysferlin, caveolin-3 and MG53 is thought to be critical for membrane repair in skeletal muscle.<ref name="pmid19380584">{{cite journal |vauthors=Cai C, Weisleder N, Ko JK, Komazaki S, Sunada Y, Nishi M, Takeshima H, Ma J |title=Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin |journal=J. Biol. Chem. |volume=284 |issue=23 |pages=15894–902 |year=2009 |pmid=19380584 |pmc=2708885 |doi=10.1074/jbc.M109.009589 |doi-access=free}}</ref>
== References ==
{{reflist|35em}}
== Further reading ==
{{refbegin|35em}}
* {{cite journal | vauthors = Bejaoui K, Hirabayashi K, Hentati F, Haines JL, Ben Hamida C, Belal S, Miller RG, McKenna-Yasek D, Weissenbach J, Rowland LP | title = Linkage of Miyoshi myopathy (distal autosomal recessive muscular dystrophy) locus to chromosome 2p12-14 | journal = Neurology | volume = 45 | issue = 4 | pages = 768–72 | year = 1995 | pmid = 7723968 | doi = 10.1212/wnl.45.4.768 | s2cid = 31029040 }}
* {{cite journal | vauthors = Bashir R, Strachan T, Keers S, Stephenson A, Mahjneh I, Marconi G, Nashef L, Bushby KM | title = A gene for autosomal recessive limb-girdle muscular dystrophy maps to chromosome 2p | journal = Hum. Mol. Genet. | volume = 3 | issue = 3 | pages = 455–7 | year = 1994 | pmid = 8012357 | doi = 10.1093/hmg/3.3.455 }}
* {{cite journal | vauthors = Liu J, Aoki M, Illa I, Wu C, Fardeau M, Angelini C, Serrano C, Urtizberea JA, Hentati F, Hamida MB, Bohlega S, Culper EJ, Amato AA, Bossie K, Oeltjen J, Bejaoui K, McKenna-Yasek D, Hosler BA, Schurr E, Arahata K, de Jong PJ, Brown RH | title = Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy | journal = Nat. Genet. | volume = 20 | issue = 1 | pages = 31–6 | year = 1998 | pmid = 9731526 | doi = 10.1038/1682 | s2cid = 12018395 }}
* {{cite journal | vauthors = Bashir R, Britton S, Strachan T, Keers S, Vafiadaki E, Lako M, Richard I, Marchand S, Bourg N, Argov Z, Sadeh M, Mahjneh I, Marconi G, Passos-Bueno MR, Moreira Ede S, Zatz M, Beckmann JS, Bushby K | title = A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B | journal = Nat. Genet. | volume = 20 | issue = 1 | pages = 37–42 | year = 1998 | pmid = 9731527 | doi = 10.1038/1689 | s2cid = 24234676 }}
* {{cite journal | vauthors = Anderson LV, Davison K, Moss JA, Young C, Cullen MJ, Walsh J, Johnson MA, Bashir R, Britton S, Keers S, Argov Z, Mahjneh I, Fougerousse F, Beckmann JS, Bushby KM | title = Dysferlin is a plasma membrane protein and is expressed early in human development | journal = Hum. Mol. Genet. | volume = 8 | issue = 5 | pages = 855–61 | year = 1999 | pmid = 10196375 | doi = 10.1093/hmg/8.5.855 | doi-access = }}
* {{cite journal | vauthors = Weiler T, Bashir R, Anderson LV, Davison K, Moss JA, Britton S, Nylen E, Keers S, Vafiadaki E, Greenberg CR, Bushby CR, Wrogemann K | title = Identical mutation in patients with limb girdle muscular dystrophy type 2B or Miyoshi myopathy suggests a role for modifier gene(s) | journal = Hum. Mol. Genet. | volume = 8 | issue = 5 | pages = 871–7 | year = 1999 | pmid = 10196377 | doi = 10.1093/hmg/8.5.871 }}
* {{cite journal | vauthors = Matsuda C, Aoki M, Hayashi YK, Ho MF, Arahata K, Brown RH | title = Dysferlin is a surface membrane-associated protein that is absent in Miyoshi myopathy | journal = Neurology | volume = 53 | issue = 5 | pages = 1119–22 | year = 1999 | pmid = 10496277 | doi = 10.1212/wnl.53.5.1119 | s2cid = 6068681 }}
* {{cite journal | vauthors = Illa I, Serrano-Munuera C, Gallardo E, Lasa A, Rojas-García R, Palmer J, Gallano P, Baiget M, Matsuda C, Brown RH | title = Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype | journal = Ann. Neurol. | volume = 49 | issue = 1 | pages = 130–4 | year = 2001 | pmid = 11198284 | doi = 10.1002/1531-8249(200101)49:1<130::AID-ANA22>3.0.CO;2-0 | s2cid = 9278818 }}
* {{cite journal | vauthors = Aoki M, Liu J, Richard I, Bashir R, Britton S, Keers SM, Oeltjen J, Brown HE, Marchand S, Bourg N, Beley C, McKenna-Yasek D, Arahata K, Bohlega S, Cupler E, Illa I, Majneh I, Barohn RJ, Urtizberea JA, Fardeau M, Amato A, Angelini C, Bushby K, Beckmann JS, Brown RH | title = Genomic organization of the dysferlin gene and novel mutations in Miyoshi myopathy | journal = Neurology | volume = 57 | issue = 2 | pages = 271–8 | year = 2001 | pmid = 11468312 | doi = 10.1212/wnl.57.2.271 | s2cid = 31959549 }}
* {{cite journal | vauthors = Matsuda C, Hayashi YK, Ogawa M, Aoki M, Murayama K, Nishino I, Nonaka I, Arahata K, Brown RH | title = The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle | journal = Hum. Mol. Genet. | volume = 10 | issue = 17 | pages = 1761–6 | year = 2001 | pmid = 11532985 | doi = 10.1093/hmg/10.17.1761 | doi-access = free }}
* {{cite journal | vauthors = Ikezoe K, Furuya H, Ohyagi Y, Osoegawa M, Nishino I, Nonaka I, Kira J | title = Dysferlin expression in tubular aggregates: their possible relationship to endoplasmic reticulum stress | journal = Acta Neuropathol. | volume = 105 | issue = 6 | pages = 603–9 | year = 2003 | pmid = 12664320 | doi = 10.1007/s00401-003-0686-1 | s2cid = 7734282 }}
* {{cite journal | vauthors = von Tell D, Bruder CE, Anderson LV, Anvret M, Ahlberg G | title = Refined mapping of the Welander distal myopathy region on chromosome 2p13 positions the new candidate region telomeric of the DYSF locus | journal = Neurogenetics | volume = 4 | issue = 4 | pages = 173–7 | year = 2003 | pmid = 12836053 | doi = 10.1007/s10048-003-0154-z | s2cid = 27539044 }}
* {{cite journal | vauthors = Lennon NJ, Kho A, Bacskai BJ, Perlmutter SL, Hyman BT, Brown RH | title = Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing | journal = J. Biol. Chem. | volume = 278 | issue = 50 | pages = 50466–73 | year = 2003 | pmid = 14506282 | doi = 10.1074/jbc.M307247200 | doi-access = free }}
* {{cite journal | vauthors = Katz JS, Rando TA, Barohn RJ, Saperstein DS, Jackson CE, Wicklund M, Amato AA | title = Late-onset distal muscular dystrophy affecting the posterior calves | journal = Muscle Nerve | volume = 28 | issue = 4 | pages = 443–8 | year = 2003 | pmid = 14506716 | doi = 10.1002/mus.10458 | s2cid = 29825709 }}
* {{cite journal | vauthors = Confalonieri P, Oliva L, Andreetta F, Lorenzoni R, Dassi P, Mariani E, Morandi L, Mora M, Cornelio F, Mantegazza R | title = Muscle inflammation and MHC class I up-regulation in muscular dystrophy with lack of dysferlin: an immunopathological study | journal = J. Neuroimmunol. | volume = 142 | issue = 1–2 | pages = 130–6 | year = 2003 | pmid = 14512171 | doi = 10.1016/S0165-5728(03)00255-8 | s2cid = 37727809 }}
* {{cite journal | vauthors = Foxton RM, Laval SH, Bushby KM | title = Characterisation of the dysferlin skeletal muscle promoter | journal = Eur. J. Hum. Genet. | volume = 12 | issue = 2 | pages = 127–31 | year = 2004 | pmid = 14560310 | doi = 10.1038/sj.ejhg.5201092 | doi-access = free }}
* {{cite journal | vauthors = Cagliani R, Fortunato F, Giorda R, Rodolico C, Bonaglia MC, Sironi M, D'Angelo MG, Prelle A, Locatelli F, Toscano A, Bresolin N, Comi GP | title = Molecular analysis of LGMD-2B and MM patients: identification of novel DYSF mutations and possible founder effect in the Italian population | journal = Neuromuscul. Disord. | volume = 13 | issue = 10 | pages = 788–95 | year = 2003 | pmid = 14678801 | doi = 10.1016/S0960-8966(03)00133-0 | s2cid = 23179310 }}
* {{cite journal | vauthors = Capanni C, Sabatelli P, Mattioli E, Ognibene A, Columbaro M, Lattanzi G, Merlini L, Minetti C, Maraldi NM, Squarzoni S | title = Dysferlin in a hyperCKaemic patient with caveolin 3 mutation and in C2C12 cells after p38 MAP kinase inhibition | journal = Exp. Mol. Med. | volume = 35 | issue = 6 | pages = 538–44 | year = 2003 | pmid = 14749532 | doi = 10.1038/emm.2003.70 | doi-access = free }}
* {{cite journal | vauthors = Brüss M, Homann J, Molderings GJ | title = [Dysferlinopathy as an extrahepatic cause for the elevation of serum transaminases] | journal = Med. Klin. (Munich) | volume = 99 | issue = 6 | pages = 326–9 | year = 2004 | pmid = 15221058 | doi = 10.1007/s00063-004-1046-1 | s2cid = 30657667 }}
* {{cite journal | vauthors = Huang Y, de Morrée A, van Remoortere A, Bushby K, Frants RR, den Dunnen JT, van der Maarel SM | title = Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle | journal = Hum. Mol. Genet. | volume = 17 | issue = 12 | pages = 1855–66 | year = 2008 | pmid = 18334579 | pmc = 2900895 | doi = 10.1093/hmg/ddn081 }}
{{refend}}
== External links ==
* [https://www.ncbi.nlm.nih.gov/books/NBK1303/ GeneReviews/NCBI/NIH/UW entry on Dysferlinopathy including Miyoshi Distal Myopathy (Miyoshi Myopathy), Limb-Girdle Muscular Dystrophy Type 2B (LGMD2B)]
* [[LOVD]] mutation database: [http://www.dmd.nl/nmdb2/?select_db=DYSF DYSF]
{{Muscle tissue}}
{{Other cell membrane proteins}}
[[Category:Proteins]]
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