Emerin

EMD
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1JEI, 2ODC, 2ODG
Identifikatori
Aliasi	EMD
Vanjski ID-jevi	OMIM: 300384 MGI: 108117 HomoloGene: 91 GeneCards: EMD
Lokacija gena (čovjek)
Hrom.	Hromosom X
Kraj	154,381,574 bp
Lokacija gena (miš)
Hrom.	Hromosom X (miš)
Kraj	73,305,154 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• GO:0001948, GO:0016582 vezivanje za proteine; • beta-tubulin binding; • actin binding; • cadherin binding;
Ćelijska komponenta	• integral component of membrane; • Jedarna membrana; • membrana; • nuclear inner membrane; • Endoplazmatski retikulum; • Mikrotubula; • nuclear outer membrane; • jedro; • nukleoplazma; • citoplazma; • nuclear envelope; • spindle pole centrosome; • cortical endoplasmic reticulum; • Diobeno vreteno;
Biološki proces	• Mišićna kontrakcija; • regulation of canonical Wnt signaling pathway; • cellular response to growth factor stimulus; • muscle organ development; • positive regulation of protein export from nucleus; • mitotic nuclear membrane disassembly; • skeletal muscle cell differentiation; • mitotic nuclear membrane reassembly; • negative regulation of fibroblast proliferation; • negative regulation of canonical Wnt signaling pathway;
	Izvori:Amigo / QuickGO
Ortolozi
	2010
	13726
	ENSG00000102119
	ENSMUSG00000001964
	P50402
	O08579
	NM_000117
	NM_007927
	NP_000108
	NP_031953
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Emerin je protein koji kod ljudi kodiran genom EMD, poznatim i kao gen STA. Emerin, zajedno sa LEMD3, sadrži integralni protein membrane koji sadrži unutrašnja jedarna membrana kod kičmenjaka. Emerin je visoko izražen u srčanom i skeletnim mišićima. U srčanom mišiću, emerin se lokalizuje na adherens spojeve unutar gmeđukaliranog diska, dje izgleda da funkcionira u mehanotransdukciji ćelijskog soja i u signalizaciji beta-katenina. Mutacije emerina uzrokuju X-vezano recesivnu Emery-Dreifussovu mišićnu distrofiju, abnormalnosti srčanog provođenja i dilatiranu kardiomiopatiju.

Ime je dobio po Alanu Emeryiju.

Struktura

Emerin je protein od 29,0 kDa (u MW 34 kDa), sastavljen od 254 aminokiseline.^[5] Emerin je serinom bogat protein sa N-krajem sa 20-aminokiselinskom hidrofobnom regijom koja je okružena nabijenim ostacima. Hidrofobna regija može biti važna za učvršćivanje proteina na membrani, s napunjenim završnim citosolnim repovima.^[6] U srčanom, skeletnom i glatkom mišiću, emerin se lokalizuje u unutrašnju jedrovu membranu;^[7]^[8] ekspresija emerina je najviša u skeletnim i srčanom mišiću.^[6] Konkretno, u srčanom mišiću, emerin se također nlazi na adherens spojevima unutar interkaliranih diskova.^[9]^[10]^[11]

Funkcija

Emerin je protein serinom bogate jedrove membrane i član porodice proteina povezane sa jedarnom laminom. Posreduje sidrenje membrane na citoskelet. Emery – Dreifussova mišićna distrofija nasljeđuje se kao X-vezana degenerativna miopatija koja je posljedica mutacije u genu EMD (također klinički poznat kao STA ).^[12] Čini se da je emerin uključen u mehanotransdukciju, jer mišji fibroblast i s nedostatkom emerina nisu uspjeli transducirati normalne reakcije ekspresije mehanosenzitivnih gena na podražaje soja.^[13] U srčanom mišiću, emerin se također nalazi u kompleksu sa beta-kateninom na adherens spoj evima interkaliranog diska. Kardiomiociti srca kojima nedostaje emerin pokazali su preraspodjelu beta-katenina, kao i poremećenu arhitekturu i oblik miocita interkaliranog diska . Ova interakcija regulirana je putem glikogen-sintaza kinaze 3 beta.^[14]

Klinički značaj

Mutacije emerina uzrokuju X-vezano recesivno Emery – Dreifussove mišićne distrofije, koje karakteriziraju rane kontrakture u Ahilovim tetivama, laktovima i postcerviksnim mišićima. Javlja se mišićna slabost. koja je proksimalna u gornjim udovima i distalna u donjim udovima; zajedno sa srčanim defektima provodljivosti koji se kreću od sinusne bradikardije, produženja zupca PR do završetka srčanim blokom.^[15] Kod ovih pacijenata imunobojenje emerina gubi se u različitim tkivima, uključujući mišiće, kožne fibroblaste i leukocita, ali dijagnostički protokoli uključuju mutacijsku analizu, a ne bojenje proteina.^[15] U gotovo svim slučajevima, mutacije rezultiraju potpunom delecijom ili neotkrivljivim nivoima emerinskog proteina. Otprilike 20% slučajeva ima X hromosome sa inverzijom unutar Xq28 regiona.^[16]

Šta više, nedavna istraživanja otkrila su da odsustvo funkcionalnog emerina može smanjiti infektivnost HIV-1. Stoga se nagađa da pacijenti koji pate od Emery-Dreifussove mišićne distrofije mogu imati imunost ili pokazati nepravilan obrazac infekcije sa HIV-1.^[17]

Interakcije

Pokazano je da emerin ima interakcije sa:

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000102119 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001964 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Protein sequence of human EMD (Uniprot ID: P50402)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Arhivirano s originala, 4. 3. 2016. Pristupljeno 16. 9. 2015.
^ ^a ^b Bione S, Maestrini E, Rivella S, Mancini M, Regis S, Romeo G, Toniolo D (Dec 1994). "Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy". Nature Genetics. 8 (4): 323–7. doi:10.1038/ng1294-323. PMID 7894480.
^ Nagano A, Koga R, Ogawa M, Kurano Y, Kawada J, Okada R, Hayashi YK, Tsukahara T, Arahata K (Mar 1996). "Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy". Nature Genetics. 12 (3): 254–9. doi:10.1038/ng0396-254. PMID 8589715.
^ Manilal S, Nguyen TM, Sewry CA, Morris GE (Jun 1996). "The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein". Human Molecular Genetics. 5 (6): 801–8. doi:10.1093/hmg/5.6.801. PMID 8776595.
^ Cartegni L, di Barletta MR, Barresi R, Squarzoni S, Sabatelli P, Maraldi N, Mora M, Di Blasi C, Cornelio F, Merlini L, Villa A, Cobianchi F, Toniolo D (Dec 1997). "Heart-specific localization of emerin: new insights into Emery–Dreifuss muscular dystrophy". Human Molecular Genetics. 6 (13): 2257–64. doi:10.1093/hmg/6.13.2257. PMID 9361031.
^ ^a ^b Wheeler MA, Warley A, Roberts RG, Ehler E, Ellis JA (Mar 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation". Cellular and Molecular Life Sciences. 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.
^ Manilal S, Sewry CA, Pereboev A, Man N, Gobbi P, Hawkes S, Love DR, Morris GE (Feb 1999). "Distribution of emerin and lamins in the heart and implications for Emery–Dreifuss muscular dystrophy". Human Molecular Genetics. 8 (2): 353–9. doi:10.1093/hmg/8.2.353. PMID 9949197.
^ "Entrez Gene: EMD emerin (Emery–Dreifuss muscular dystrophy)".
^ Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29. 8. 2005). "Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells". The Journal of Cell Biology. 170 (5): 781–91. doi:10.1083/jcb.200502148. PMC 2171355. PMID 16115958.
^ Wheeler, MA; Warley, A; Roberts, RG; Ehler, E; Ellis, JA (mart 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation". Cellular and Molecular Life Sciences. 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.
^ ^a ^b Emery AE (Jun 2000). "Emery–Dreifuss muscular dystrophy - a 40 year retrospective". Neuromuscular Disorders. 10 (4–5): 228–32. doi:10.1016/s0960-8966(00)00105-x. PMID 10838246.
^ Small K, Warren ST (Jan 1998). "Emerin deletions occurring on both Xq28 inversion backgrounds". Human Molecular Genetics. 7 (1): 135–9. doi:10.1093/hmg/7.1.135. PMID 9384614.
^ Li M, Craigie R (Jun 2006). "Virology: HIV goes nuclear". Nature. 441 (7093): 581–2. Bibcode:2006Natur.441..581L. doi:10.1038/441581a. PMID 16738646.
^ ^a ^b ^c Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (Apr 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochemical and Biophysical Research Communications. 303 (3): 764–70. doi:10.1016/s0006-291x(03)00415-7. PMID 12670476.
^ Berk JM, Simon DN, Jenkins-Houk CR, Westerbeck JW, Grønning-Wang LM, Carlson CR, Wilson KL (Sep 2014). "The molecular basis of emerin-emerin and emerin-BAF interactions". Journal of Cell Science. 127 (Pt 18): 3956–69. doi:10.1242/jcs.148247. PMC 4163644. PMID 25052089.
^ ^a ^b Holaska JM, Lee KK, Kowalski AK, Wilson KL (Feb 2003). "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro". The Journal of Biological Chemistry. 278 (9): 6969–75. doi:10.1074/jbc.M208811200. PMID 12493765.
^ Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y (Mar 2004). "Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy". European Journal of Biochemistry / FEBS. 271 (5): 1035–45. doi:10.1111/j.1432-1033.2004.04007.x. PMID 15009215.
^ Markiewicz E, Tilgner K, Barker N, van de Wetering M, Clevers H, Dorobek M, Hausmanowa-Petrusewicz I, Ramaekers FC, Broers JL, Blankesteijn WM, Salpingidou G, Wilson RG, Ellis JA, Hutchison CJ (Jul 2006). "The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus". The EMBO Journal. 25 (14): 3275–85. doi:10.1038/sj.emboj.7601230. PMC 1523183. PMID 16858403.
^ ^a ^b ^c Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE (Jun 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". European Journal of Biochemistry / FEBS. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
^ Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (Feb 2001). "Interaction between emerin and nuclear lamins". Journal of Biochemistry. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
^ Clements L, Manilal S, Love DR, Morris GE (Jan 2000). "Direct interaction between emerin and lamin A". Biochemical and Biophysical Research Communications. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.
^ ^a ^b Zhang Q, Skepper JN, Yang F, Davies JD, Hegyi L, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM (Dec 2001). "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues". Journal of Cell Science. 114 (Pt 24): 4485–98. PMID 11792814.
^ Mislow JM, Holaska JM, Kim MS, Lee KK, Segura-Totten M, Wilson KL, McNally EM (Aug 2002). "Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro". FEBS Letters. 525 (1–3): 135–40. doi:10.1016/s0014-5793(02)03105-8. PMID 12163176.
^ ^a ^b Wheeler MA, Davies JD, Zhang Q, Emerson LJ, Hunt J, Shanahan CM, Ellis JA (Aug 2007). "Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy". Experimental Cell Research. 313 (13): 2845–57. doi:10.1016/j.yexcr.2007.03.025. PMID 17462627.
^ Zhang Q, Ragnauth CD, Skepper JN, Worth NF, Warren DT, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM (Feb 2005). "Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle". Journal of Cell Science. 118 (Pt 4): 673–87. doi:10.1242/jcs.01642. PMID 15671068.
^ Bengtsson L, Otto H (Feb 2008). "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane". Journal of Cell Science. 121 (Pt 4): 536–48. doi:10.1242/jcs.019281. PMID 18230648.

Dopunska literatura

Gant TM, Wilson KL (1998). "Nuclear assembly". Annu. Rev. Cell Dev. Biol. 13: 669–95. doi:10.1146/annurev.cellbio.13.1.669. PMID 9442884.
Helbling-Leclerc A, Bonne G, Schwartz K (2002). "Emery–Dreifuss muscular dystrophy". Eur. J. Hum. Genet. 10 (3): 157–61. doi:10.1038/sj.ejhg.5200744. PMID 11973618.
Holaska JM, Wilson KL (2006). "Multiple roles for emerin: implications for Emery–Dreifuss muscular dystrophy". The Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology. 288 (7): 676–80. doi:10.1002/ar.a.20334. PMC 2559942. PMID 16761279.
Bione S, Tamanini F, Maestrini E, Tribioli C, Poustka A, Torri G, Rivella S, Toniolo D (1994). "Transcriptional organization of a 450-kb region of the human X chromosome in Xq28". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 10977–81. doi:10.1073/pnas.90.23.10977. PMC 47904. PMID 8248200.
Bione S, Small K, Aksmanovic VM, D'Urso M, Ciccodicola A, Merlini L, Morandi L, Kress W, Yates JR, Warren ST (1996). "Identification of new mutations in the Emery–Dreifuss muscular dystrophy gene and evidence for genetic heterogeneity of the disease". Hum. Mol. Genet. 4 (10): 1859–63. doi:10.1093/hmg/4.10.1859. PMID 8595407.
Yamada T, Kobayashi T (1996). "A novel emerin mutation in a Japanese patient with Emery–Dreifuss muscular dystrophy". Hum. Genet. 97 (5): 693–4. doi:10.1007/BF02281886. PMID 8655156.
Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L, Heiner C, Burough F, Repetto M, Schlessinger D, D'Urso M (1997). "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci". Hum. Mol. Genet. 5 (5): 659–68. doi:10.1093/hmg/5.5.659. PMID 8733135.
Ellis JA, Craxton M, Yates JR, Kendrick-Jones J (1998). "Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery–Dreifuss muscular dystrophy phenotype". J. Cell Sci. 111 (6): 781–92. PMID 9472006.
Squarzoni S, Sabatelli P, Ognibene A, Toniolo D, Cartegni L, Cobianchi F, Petrini S, Merlini L, Maraldi NM (1998). "Immunocytochemical detection of emerin within the nuclear matrix". Neuromuscul. Disord. 8 (5): 338–44. doi:10.1016/S0960-8966(98)00031-5. PMID 9673989.
Ellis JA, Yates JR, Kendrick-Jones J, Brown CA (1999). "Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery–Dreifuss muscular dystrophy". Hum. Genet. 104 (3): 262–8. doi:10.1007/s004390050946. PMID 10323252.
Squarzoni S, Sabatelli P, Capanni C, Petrini S, Ognibene A, Toniolo D, Cobianchi F, Zauli G, Bassini A, Baracca A, Guarnieri C, Merlini L, Maraldi NM (2001). "Emerin presence in platelets". Acta Neuropathol. 100 (3): 291–8. doi:10.1007/s004019900169. PMID 10965799.
Martins SB, Eide T, Steen RL, Jahnsen T, Skålhegg BS, Collas P (2001). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". J. Cell Sci. 113 (21): 3703–13. PMID 11034899.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Laguri C, Gilquin B, Wolff N, Romi-Lebrun R, Courchay K, Callebaut I, Worman HJ, Zinn-Justin S (2001). "Structural characterization of the LEM motif common to three human inner nuclear membrane proteins". Structure. 9 (6): 503–11. doi:10.1016/S0969-2126(01)00611-6. PMID 11435115.

Vanjski linkovi

GeneReviews/NCBI/NIH/UW entry on Emery–Dreifuss muscular dystrophy
EMD protein, human na US National Library of Medicine Medical Subject Headings (MeSH)

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000102119 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000001964 - 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] "Protein sequence of human EMD (Uniprot ID: P50402)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Arhivirano s originala, 4. 3. 2016. Pristupljeno 16. 9. 2015.

[ReferenceA-6] Bione S, Maestrini E, Rivella S, Mancini M, Regis S, Romeo G, Toniolo D (Dec 1994). "Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy". Nature Genetics. 8 (4): 323–7. doi:10.1038/ng1294-323. PMID 7894480.

[7] Nagano A, Koga R, Ogawa M, Kurano Y, Kawada J, Okada R, Hayashi YK, Tsukahara T, Arahata K (Mar 1996). "Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy". Nature Genetics. 12 (3): 254–9. doi:10.1038/ng0396-254. PMID 8589715.

[8] Manilal S, Nguyen TM, Sewry CA, Morris GE (Jun 1996). "The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein". Human Molecular Genetics. 5 (6): 801–8. doi:10.1093/hmg/5.6.801. PMID 8776595.

[9] Cartegni L, di Barletta MR, Barresi R, Squarzoni S, Sabatelli P, Maraldi N, Mora M, Di Blasi C, Cornelio F, Merlini L, Villa A, Cobianchi F, Toniolo D (Dec 1997). "Heart-specific localization of emerin: new insights into Emery–Dreifuss muscular dystrophy". Human Molecular Genetics. 6 (13): 2257–64. doi:10.1093/hmg/6.13.2257. PMID 9361031.

[Wheeler_2010-10] Wheeler MA, Warley A, Roberts RG, Ehler E, Ellis JA (Mar 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation". Cellular and Molecular Life Sciences. 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.

[11] Manilal S, Sewry CA, Pereboev A, Man N, Gobbi P, Hawkes S, Love DR, Morris GE (Feb 1999). "Distribution of emerin and lamins in the heart and implications for Emery–Dreifuss muscular dystrophy". Human Molecular Genetics. 8 (2): 353–9. doi:10.1093/hmg/8.2.353. PMID 9949197.

[entrez-12] "Entrez Gene: EMD emerin (Emery–Dreifuss muscular dystrophy)".

[13] Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29. 8. 2005). "Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells". The Journal of Cell Biology. 170 (5): 781–91. doi:10.1083/jcb.200502148. PMC 2171355. PMID 16115958.

[14] Wheeler, MA; Warley, A; Roberts, RG; Ehler, E; Ellis, JA (mart 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation". Cellular and Molecular Life Sciences. 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.

[ReferenceB-15] Emery AE (Jun 2000). "Emery–Dreifuss muscular dystrophy - a 40 year retrospective". Neuromuscular Disorders. 10 (4–5): 228–32. doi:10.1016/s0960-8966(00)00105-x. PMID 10838246.

[16] Small K, Warren ST (Jan 1998). "Emerin deletions occurring on both Xq28 inversion backgrounds". Human Molecular Genetics. 7 (1): 135–9. doi:10.1093/hmg/7.1.135. PMID 9384614.

[17] Li M, Craigie R (Jun 2006). "Virology: HIV goes nuclear". Nature. 441 (7093): 581–2. Bibcode:2006Natur.441..581L. doi:10.1038/441581a. PMID 16738646.

[pmid12670476-18] Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (Apr 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochemical and Biophysical Research Communications. 303 (3): 764–70. doi:10.1016/s0006-291x(03)00415-7. PMID 12670476.

[19] Berk JM, Simon DN, Jenkins-Houk CR, Westerbeck JW, Grønning-Wang LM, Carlson CR, Wilson KL (Sep 2014). "The molecular basis of emerin-emerin and emerin-BAF interactions". Journal of Cell Science. 127 (Pt 18): 3956–69. doi:10.1242/jcs.148247. PMC 4163644. PMID 25052089.

[Holaska_2003-20] Holaska JM, Lee KK, Kowalski AK, Wilson KL (Feb 2003). "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro". The Journal of Biological Chemistry. 278 (9): 6969–75. doi:10.1074/jbc.M208811200. PMID 12493765.

[21] Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y (Mar 2004). "Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy". European Journal of Biochemistry / FEBS. 271 (5): 1035–45. doi:10.1111/j.1432-1033.2004.04007.x. PMID 15009215.

[22] Markiewicz E, Tilgner K, Barker N, van de Wetering M, Clevers H, Dorobek M, Hausmanowa-Petrusewicz I, Ramaekers FC, Broers JL, Blankesteijn WM, Salpingidou G, Wilson RG, Ellis JA, Hutchison CJ (Jul 2006). "The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus". The EMBO Journal. 25 (14): 3275–85. doi:10.1038/sj.emboj.7601230. PMC 1523183. PMID 16858403.

[pmid12755701-23] Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE (Jun 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". European Journal of Biochemistry / FEBS. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.

[pmid11173535-24] Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (Feb 2001). "Interaction between emerin and nuclear lamins". Journal of Biochemistry. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.

[pmid10673356-25] Clements L, Manilal S, Love DR, Morris GE (Jan 2000). "Direct interaction between emerin and lamin A". Biochemical and Biophysical Research Communications. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.

[Zhang_2001-26] Zhang Q, Skepper JN, Yang F, Davies JD, Hegyi L, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM (Dec 2001). "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues". Journal of Cell Science. 114 (Pt 24): 4485–98. PMID 11792814.

[27] Mislow JM, Holaska JM, Kim MS, Lee KK, Segura-Totten M, Wilson KL, McNally EM (Aug 2002). "Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro". FEBS Letters. 525 (1–3): 135–40. doi:10.1016/s0014-5793(02)03105-8. PMID 12163176.

[Wheeler_2007-28] Wheeler MA, Davies JD, Zhang Q, Emerson LJ, Hunt J, Shanahan CM, Ellis JA (Aug 2007). "Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy". Experimental Cell Research. 313 (13): 2845–57. doi:10.1016/j.yexcr.2007.03.025. PMID 17462627.

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