Disferlin

DYSF
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 4CAH, 4CAI, 4IHB, 4IQH
Identifikatori
Aliasi	DYSF, FER1L1, LGMD2B, MMD1, disferlin, LGMDR2
Vanjski ID-jevi	OMIM: 603009 MGI: 1349385 HomoloGene: 20748 GeneCards: DYSF
Lokacija gena (čovjek) Hrom. Hromosom 2 (čovjek)[1] Bend 2p13.2 Početak 71,453,561 bp[1] Kraj 71,686,763 bp[1]
Lokacija gena (miš) Hrom. Hromosom 6 (miš)[2] Bend 6 C3|6 36.14 cM Početak 83,985,572 bp[2] Kraj 84,188,042 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • calcium ion binding • vezivanje iona metala • GO:0001948, GO:0016582 vezivanje za proteine • calcium-dependent phospholipid binding • phospholipid binding • lipid binding • microtubule binding • alpha-tubulin binding Ćelijska komponenta • integral component of membrane • endozom • late endosome • membrana • T-tubule • ćelijska membrana • endocytic vesicle • early endosome • Sarkolema • Egzosom • cytoplasmic vesicle membrane • GO:0016023 citoplazmatska vezikula • lamellipodium • centar organizacije mikrotubula • jedro • Golđijev aparat • Mikrotubula • membrane microdomain Biološki proces • Mišićna kontrakcija • plasma membrane repair • Fuzija vezikula • Angiogeneza • positive regulation of endothelial cell proliferation • monocyte activation involved in immune response • macrophage activation involved in immune response • glycerol metabolic process • negative regulation of gene expression • lipid storage • T-tubule organization • GO:1903363 negative regulation of protein catabolic process • skeletal muscle tissue regeneration • fat cell differentiation • positive regulation of cell adhesion • negative regulation of phagocytosis • cellular response to osmotic stress • positive regulation of neutrophil chemotaxis • regulation of calcium ion import • negative regulation of high voltage-gated calcium channel activity • negative regulation of protein polyubiquitination Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	8291	26903
Ensembl	ENSG00000135636	ENSMUSG00000033788
UniProt	O75923	Q9ESD7
RefSeq (mRNK)	NM_001130455 NM_001130976 NM_001130977 NM_001130978 NM_001130979 NM_001130980 NM_001130981 NM_001130982 NM_001130983 NM_001130984 NM_001130985 NM_001130986 NM_001130987 NM_003494	NM_001077694 NM_021469 NM_001310152
RefSeq (bjelančevina)	NP_001123927 NP_001124448 NP_001124449 NP_001124450 NP_001124451 NP_001124452 NP_001124453 NP_001124454 NP_001124455 NP_001124456 NP_001124457 NP_001124458 NP_001124459 NP_003485	NP_001071162 NP_001297081 NP_067444 NP_001390584 NP_001390585 NP_001390586 NP_001390587
Lokacija (UCSC)	Chr 2: 71.45 – 71.69 Mb	Chr 6: 83.99 – 84.19 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Disferlin, poznat i kao distrofija-vezani fer-1-protein je protein koji je kod ljudi kodiran od' gen DYSF.^[5]

Disferlin je povezan sa popravkom skeletnih mišića.^[6] Defekt u DYSF genu, koji se nalazi na hromosomu 2, pozocija p12-14, izaziva nekoliko tipova mišićne distrofije, uključujući Miyoshi miopatiju (MM), distrofiju udova i pojasa tip 2B (LGMD2B) i distalnu miopatiju (DM). Smanjenje ili odsustvo disferlina, nazvano disferlinopatija, obično postaje očigledno u trećoj ili četvrtoj deceniji života, a karakterizira ga slabost i gubljenje različitih hotimičnih pokreta skeletnih mišića.^[7]

Struktura

Ferlin family
Identifikatori
Simbol	Dysferlin
OPM superporodica	452
OPM protein	4cah

Ljudski protein disferlin je transmembranski protein od 237 kilodaltona tipa II.^{[8][9][10][11][12]} Sadrži velik unutarćelijski citoplazmatski domen N-kraja, ekstremni C-krajev transmembranski domen i kratki C-krajev vanćelijski domen. Citosolni domen disferlina sastoji se od sedam visoko konzerviranih C2-domena (C2A-G), koji su konzervirani u nekoliko proteina unutar porodice ferlina, uključujući homolog disferlina – mioferlin.^[13][14] U stvari, C2 domen na bilo kojem datom položaju sličniji je C2 domenu na odgovarajućem položaju unutar ostalih članova porodice ferlina nego susjedni C2-domen unutar istog proteina. To sugerira da svaki pojedinačni C2-domen u stvari može imati određenu ulogu u funkciji disferlina. Riješena je kristalna struktura C2A-domena ljudskog disferlina i otkrila da C2A domen mijenja konformaciju u interakciji s kalcijskim ionima, što je u skladu sa sve većim brojem dokaza koji sugeriraju da C2A-domen ima ulogu u vezanju lipida ovisno o kalciju.^[15] In addition to the C2 domains, dysferlin also contains "FerA" and "DysF" domains. Mutations in both FerA^[16] and DysF^[17] Može izazvati mišićne distrofije. DysF domen ima zanimljivu strukturu, jer sadrži jedan DysF domen unutar drugog DysF domena, što je posljedica umnožavanja gena; međutim, funkcija ovog domena do sada nije poznata. FerA domen je očuvan među svim članovima porodice ferlinskih proteina. Postoje dvije mutacije u Ferfer domenu disferlina koje su povezane s mišićnom distrofijom. FerA domen je snop od četiri zavojnice i može komunicirati s membranom, obično ovisno o kalciju.

Funkcija

Uloga disferlina najintenzivnije se proučava u ćelijskom procesu koji se naziva popravak membrane. Popravak membrane je presudan mehanizam pomoću kojeg ćelije mogu začepiti dramatične rane na plazmatskoj membrani. Smatra se da je mišić posebno sklon ranama na membrani s obzirom na to da mišićne ćelije prenose veliku silu i prolaze kroz cikluse kontrakcije. Disferlin je visoko eksprimiran u mišićima i homologan je porodici ferlinskih proteina, za koje se smatra da reguliraju fuziju membrane u širokom spektru vrsta i ćelijskih tipova.^[18] Nekoliko linija dokaza sugerira da bi disferlin mogao biti uključen u popravak membrane u mišićima. Prvo, mišićna vlakna sa nedostatkom disferlina pokazuju nakupljanje vezikula (koje su kritične za popravak membrane kod tipova mišićnih ćelija) u blizini membranskih lezija, što ukazuje da bi disferlin mogao biti potreban za fuziju popravnih vezikula s plazmatskom membranom. Nadalje, mišićna vlakna s nedostatkom disferlina u većoj mjeri uzimaju vanćelijske boje od mišićnih vlakana divljeg tipa, nakon ranjavanja izazvanog laserom in vitro.^[19] Disferlin je također na lezijama membrane značajno obogaćen sa nekoliko dodatnih proteina, za koje se smatra da su uključeni u ponovno zaptivanje membrane, uključujući aneksin i MG53.^[20] U stvari, kako disferlin doprinosi ponovnom zaptivanju membrane nije jasno, ali biohemijski dokazi ukazuju na to da može vezati lipide na način koji zavisi od kalcija, u skladu s ulogom disferlina u regulaciji fuzije popravnih vezikula sa sarkolemom, tokom popravljanja membrane.^[21] Pored toga, snimanje miotubula koje eksferiraju disferlin-eGFP na živim ćelijama ukazuje da se disferlin lokalizira u ćelijskom odjeljku koji reagira na ozljedu, stvaranjem velikih vezikula koje sadrže disferlin, a stvaranje tih vezikula može doprinijeti saniranju rane.^[22] Dysferlin may also be involved in Alzheimer's disease pathogenesis.^[23]

Interakcije

Pokazano je da disferlin ima interakcije sa kaveolinom 3 u skeletnim mišićima,^[24] a smatra se da ova interakcija zadržava disferlin u plazmatskoj membrani.^[25] 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.^[26]

Također pogledajte

• Mišićna distrofija

Referenc

1. GRCh38: Ensembl release 89: ENSG00000135636 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033788 - Ensembl, maj 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Passos-Bueno MR, Richard I, Vainzof M, Fougerousse F, Weissenbach J, Broux O, Cohen D, Akiyama J, Marie SK, Carvalho AA (maj 1993). "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 of Medical Genetics. 30 (5): 385–7. doi:10.1136/jmg.30.5.385. PMC 1016373. PMID 8320700.
6. "Entrez Gene: DYSF dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)".
7. Leiden University Medical Center, Center for Human and Clinical Genetics - Dysferlin Retrieved 21 June 2007.
8. Kawahara, Genri; Serafini, Peter R.; Myers, Jennifer A.; Alexander, Matthew S.; Kunkel, Louis M. (23. 9. 2011). "Characterization of zebrafish dysferlin by morpholino knockdown". Biochemical and Biophysical Research Communications. 413 (2): 358–363. doi:10.1016/j.bbrc.2011.08.105. ISSN 1090-2104. PMC 4526276. PMID 21893049.
9. Fuson, Kerry; Rice, Anne; Mahling, Ryan; Snow, Adam; Nayak, Kamakshi; Shanbhogue, Prajna; Meyer, Austin G.; Redpath, Gregory M. I.; Hinderliter, Anne (7. 1. 2014). "Alternate splicing of dysferlin C2A confers Ca²⁺-dependent and Ca²⁺-independent binding for membrane repair". Structure. 22 (1): 104–115. doi:10.1016/j.str.2013.10.001. ISSN 1878-4186. PMC 5993433. PMID 24239457.
10. Demonbreun, Alexis R.; Allen, Madison V.; Warner, James L.; Barefield, David Y.; Krishnan, Swathi; Swanson, Kaitlin E.; Earley, Judy U.; McNally, Elizabeth M. (juni 2016). "Enhanced Muscular Dystrophy from Loss of Dysferlin Is Accompanied by Impaired Annexin A6 Translocation after Sarcolemmal Disruption". The American Journal of Pathology. 186 (6): 1610–1622. doi:10.1016/j.ajpath.2016.02.005. ISSN 1525-2191. PMC 4901136. PMID 27070822.
11. Cacciottolo, Mafalda; Numitone, Gelsomina; Aurino, Stefania; Caserta, Imma Rosaria; Fanin, Marina; Politano, Luisa; Minetti, Carlo; Ricci, Enzo; Piluso, Giulio (septembar 2011). "Muscular dystrophy with marked Dysferlin deficiency is consistently caused by primary dysferlin gene mutations". European Journal of Human Genetics. 19 (9): 974–980. doi:10.1038/ejhg.2011.70. ISSN 1476-5438. PMC 3179367. PMID 21522182.
12. Matsuda, Chie; Kiyosue, Kazuyuki; Nishino, Ichizo; Goto, Yuichi; Hayashi, Yukiko K. (29. 10. 2015). "Dysferlinopathy Fibroblasts Are Defective in Plasma Membrane Repair". PLOS Currents. 7. doi:10.1371/currents.md.5865add2d766f39a0e0411d38a7ba09c. ISSN 2157-3999. PMC 4639325. PMID 26579332.
13. Vafiadaki E, Reis A, Keers S, Harrison R, Anderson LV, Raffelsberger T, Ivanova S, Hoger H, Bittner RE, Bushby K, Bashir R (2001). "Cloning of the mouse dysferlin gene and genomic characterization of the SJL-Dysf mutation". NeuroReport. 12 (3): 625–9. doi:10.1097/00001756-200103050-00039. PMID 11234777.
14. Abdullah, Nazish; Padmanarayana, Murugesh; Marty, Naomi J.; Johnson, Colin P. (21. 1. 2014). "Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin". Biophysical Journal. 106 (2): 382–389. Bibcode:2014BpJ...106..382A. doi:10.1016/j.bpj.2013.11.4492. ISSN 1542-0086. PMC 3907215. PMID 24461013.
15. Therrien C, Di Fulvio S, Pickles S, Sinnreich M (2009). "Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides". Biochemistry. 48 (11): 2377–84. doi:10.1021/bi802242r. PMID 19253956.
16. Harsini, Faraz M.; Chebrolu, Sukanya; Fuson, Kerry L.; White, Mark A.; Rice, Anne M.; Sutton, R. Bryan (19. 7. 2018). "FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins". Scientific Reports. 8 (1): 10949. Bibcode:2018NatSR...810949H. doi:10.1038/s41598-018-29184-1. ISSN 2045-2322. PMC 6053371. PMID 30026467.
17. Sula, Altin; Cole, Ambrose R.; Yeats, Corin; Orengo, Christine; Keep, Nicholas H. (17. 1. 2014). "Crystal structures of the human Dysferlin inner DysF domain". BMC Structural Biology. 14: 3. doi:10.1186/1472-6807-14-3. ISSN 1472-6807. PMC 3898210. PMID 24438169.
18. 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 (1998). "A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B". Nat. Genet. 20 (1): 37–42. doi:10.1038/1689. PMID 9731527.
19. Bansal D, Miyake K, Vogel SS, Groh S, Chen CC, Williamson R, McNeil PL, Campbell KP (2003). "Defective membrane repair in dysferlin-deficient muscular dystrophy". Nature. 423 (6936): 168–72. Bibcode:2003Natur.423..168B. doi:10.1038/nature01573. PMID 12736685.
20. Roostalu U, Strähle U (2012). "In vivo imaging of molecular interactions at damaged sarcolemma". Dev. Cell. 22 (3): 515–29. doi:10.1016/j.devcel.2011.12.008. PMID 22421042.
21. Abdullah N, Padmanarayana M, Marty NJ, Johnson CP (2014). "Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin". Biophys. J. 106 (2): 382–9. Bibcode:2014BpJ...106..382A. doi:10.1016/j.bpj.2013.11.4492. PMC 3907215. PMID 24461013.
22. McDade JR, Michele DE (2014). "Membrane damage-induced vesicle-vesicle fusion of dysferlin-containing vesicles in muscle cells requires microtubules and kinesin". Hum. Mol. Genet. 23 (7): 1677–86. doi:10.1093/hmg/ddt557. PMC 3943514. PMID 24203699.
23. Chen JA, Wang Q, Davis-Turak J, et al. (april 2015). "A multiancestral genome-wide exome array study of Alzheimer disease, frontotemporal dementia, and progressive supranuclear palsy". JAMA Neurology. 72 (4): 414–22. doi:10.1001/jamaneurol.2014.4040. PMC 4397175. PMID 25706306.
24. Matsuda C, Hayashi YK, Ogawa M, Aoki M, Murayama K, Nishino I, Nonaka I, Arahata K, Brown RH (august 2001). "The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle". Hum. Mol. Genet. 10 (17): 1761–6. doi:10.1093/hmg/10.17.1761. PMID 11532985.
25. Hernández-Deviez DJ, Howes MT, Laval SH, Bushby K, Hancock JF, Parton RG (2008). "Caveolin regulates endocytosis of the muscle repair protein, dysferlin" (PDF). J. Biol. Chem. 283 (10): 6476–88. doi:10.1074/jbc.M708776200. PMID 18096699.
26. Cai C, Weisleder N, Ko JK, Komazaki S, Sunada Y, Nishi M, Takeshima H, Ma J (2009). "Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin". J. Biol. Chem. 284 (23): 15894–902. doi:10.1074/jbc.M109.009589. PMC 2708885. PMID 19380584.

Dopunska literatura

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• Bashir R, Strachan T, Keers S, Stephenson A, Mahjneh I, Marconi G, Nashef L, Bushby KM (1994). "A gene for autosomal recessive limb-girdle muscular dystrophy maps to chromosome 2p". Hum. Mol. Genet. 3 (3): 455–7. doi:10.1093/hmg/3.3.455. PMID 8012357.
• 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 (1998). "Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy". Nat. Genet. 20 (1): 31–6. doi:10.1038/1682. PMID 9731526.
• 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 (1998). "A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B". Nat. Genet. 20 (1): 37–42. doi:10.1038/1689. PMID 9731527.
• 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 (1999). "Dysferlin is a plasma membrane protein and is expressed early in human development". Hum. Mol. Genet. 8 (5): 855–61. doi:10.1093/hmg/8.5.855. PMID 10196375.
• Weiler T, Bashir R, Anderson LV, Davison K, Moss JA, Britton S, Nylen E, Keers S, Vafiadaki E, Greenberg CR, Bushby CR, Wrogemann K (1999). "Identical mutation in patients with limb girdle muscular dystrophy type 2B or Miyoshi myopathy suggests a role for modifier gene(s)". Hum. Mol. Genet. 8 (5): 871–7. doi:10.1093/hmg/8.5.871. PMID 10196377.
• Matsuda C, Aoki M, Hayashi YK, Ho MF, Arahata K, Brown RH (1999). "Dysferlin is a surface membrane-associated protein that is absent in Miyoshi myopathy". Neurology. 53 (5): 1119–22. doi:10.1212/wnl.53.5.1119. PMID 10496277.
• Illa I, Serrano-Munuera C, Gallardo E, Lasa A, Rojas-García R, Palmer J, Gallano P, Baiget M, Matsuda C, Brown RH (2001). "Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype". Ann. Neurol. 49 (1): 130–4. doi:10.1002/1531-8249(200101)49:1<130::AID-ANA22>3.0.CO;2-0. PMID 11198284.
• 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 (2001). "Genomic organization of the dysferlin gene and novel mutations in Miyoshi myopathy". Neurology. 57 (2): 271–8. doi:10.1212/wnl.57.2.271. PMID 11468312.
• Matsuda C, Hayashi YK, Ogawa M, Aoki M, Murayama K, Nishino I, Nonaka I, Arahata K, Brown RH (2001). "The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle". Hum. Mol. Genet. 10 (17): 1761–6. doi:10.1093/hmg/10.17.1761. PMID 11532985.
• Ikezoe K, Furuya H, Ohyagi Y, Osoegawa M, Nishino I, Nonaka I, Kira J (2003). "Dysferlin expression in tubular aggregates: their possible relationship to endoplasmic reticulum stress". Acta Neuropathol. 105 (6): 603–9. doi:10.1007/s00401-003-0686-1. PMID 12664320.
• von Tell D, Bruder CE, Anderson LV, Anvret M, Ahlberg G (2003). "Refined mapping of the Welander distal myopathy region on chromosome 2p13 positions the new candidate region telomeric of the DYSF locus". Neurogenetics. 4 (4): 173–7. doi:10.1007/s10048-003-0154-z. PMID 12836053.
• Lennon NJ, Kho A, Bacskai BJ, Perlmutter SL, Hyman BT, Brown RH (2003). "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing". J. Biol. Chem. 278 (50): 50466–73. doi:10.1074/jbc.M307247200. PMID 14506282.
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• Foxton RM, Laval SH, Bushby KM (2004). "Characterisation of the dysferlin skeletal muscle promoter". Eur. J. Hum. Genet. 12 (2): 127–31. doi:10.1038/sj.ejhg.5201092. PMID 14560310.
• 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 (2003). "Molecular analysis of LGMD-2B and MM patients: identification of novel DYSF mutations and possible founder effect in the Italian population". Neuromuscul. Disord. 13 (10): 788–95. doi:10.1016/S0960-8966(03)00133-0. PMID 14678801.
• Capanni C, Sabatelli P, Mattioli E, Ognibene A, Columbaro M, Lattanzi G, Merlini L, Minetti C, Maraldi NM, Squarzoni S (2003). "Dysferlin in a hyperCKaemic patient with caveolin 3 mutation and in C2C12 cells after p38 MAP kinase inhibition". Exp. Mol. Med. 35 (6): 538–44. doi:10.1038/emm.2003.70. PMID 14749532.
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Vanjski linkovi

• GeneReviews/NCBI/NIH/UW entry on Dysferlinopathy including Miyoshi Distal Myopathy (Miyoshi Myopathy), Limb-Girdle Muscular Dystrophy Type 2B (LGMD2B)
• LOVD mutation database: DYSF

Šablon:Proteini ćelijske membrane