Α-辅肌动蛋白2

Α-辅肌动蛋白2
已知的結構
PDB	直系同源搜索: PDBe RCSB
PDBID列表
	1H8B、1HCI、1QUU、4D1E、5A37、5A36、5A38、5A4B
識別號
别名	ACTN2；, CMD1AA, CMH23, actinin alpha 2, MYOCOZ, MPD6
外部ID	OMIM：102573 MGI：109192 HomoloGene：31016 GeneCards：ACTN2
相關疾病
	牙周炎、dilated cardiomyopathy 1AA
基因位置（人类）
染色体	1號染色體
终止	236,764,631 bp
基因位置（小鼠）
染色体	小鼠13号染色体
终止	12,355,641 bp
RNA表达模式
	; ; ; ;
	查阅更多表达数据
基因本體
分子功能	• calcium ion binding; • protein dimerization activity; • protein homodimerization activity; • transmembrane transporter binding; • protein domain specific binding; • titin Z domain binding; • LIM domain binding; • titin binding; • 金屬離子結合; • cytoskeletal protein binding; • integrin binding; • actin filament binding; • 血浆蛋白结合; • nuclear receptor coactivator activity; • 相同蛋白质结合; • FATZ binding; • actin binding; • phosphatidylinositol-4,5-bisphosphate binding; • structural constituent of muscle;
細胞組分	• 細胞質; • 细胞质基质; • 偽足; • 粘着斑; • 絲狀偽足; • 细胞膜; • 肌节; • 树突棘; • 細胞外區域; • Z disc; • cortical actin cytoskeleton; • 微丝; • 外排體; • 细胞骨架; • platelet alpha granule lumen; • postsynaptic density membrane; • glutamatergic synapse; • postsynaptic density, intracellular component;
生物學過程	• positive regulation of cation channel activity; • regulation of apoptotic process; • 肌肉收缩; • positive regulation of potassium ion transport; • phospholipase C-activating angiotensin-activated signaling pathway; • cardiac muscle cell development; • regulation of membrane potential; • platelet degranulation; • actin filament uncapping; • MAPK cascade; • focal adhesion assembly; • negative regulation of protein localization to cell surface; • positive regulation of signaling receptor activity; • 細胞粘附; • negative regulation of potassium ion transmembrane transporter activity; • negative regulation of potassium ion transport; • regulation of nucleic acid-templated transcription; • microspike assembly; • positive regulation of endocytic recycling; • muscle filament sliding; • protein homotetramerization; • sarcomere organization; • positive regulation of potassium ion transmembrane transporter activity; • protein localization to plasma membrane; • positive regulation of nucleic acid-templated transcription; • regulation of NMDA receptor activity;
	Sources:Amigo / QuickGO
直系同源
	88
	11472
	ENSG00000077522
	ENSMUSG00000052374
	P35609
	Q9JI91
	NM_001103; NM_001278343; NM_001278344
	NM_033268
	NP_001094; NP_001265272; NP_001265273
	NP_150371
	維基數據
檢視/編輯人類	檢視/編輯小鼠

α-辅肌动蛋白2（英語：Alpha-actinin-2）是一种蛋白质，在人类中由ACTN2基因编码。^[6]该基因编码一种在骨骼肌和心肌中表达的α-辅肌动蛋白异构体，其功能是将肌原纤维肌动蛋白细丝和肌联蛋白锚定到Z盘上。

结构

α-辅肌动蛋白2是一种103.8kDa的蛋白质，由894个氨基酸组成。^[7]^[8]每个分子都是棒状的（长度为35nm），并且以反平行的方式同源二聚化。每个单体都有一个N端肌动蛋白结合区，由两个钙调理蛋白同源结构域、两个C端 EF手结构域和四个串联血影蛋白样重复序列组成，形成分子中心区域的杆状结构域。^[9] 人类α-辅肌动蛋白2在3.5Å处的高分辨率晶体结构最近得到解决。^[10]α辅肌动蛋白属于血影蛋白基因超家族，它代表一组不同的肌动蛋白结合细胞骨架蛋白，包括血影蛋白、抗肌萎缩蛋白、肌营养相关蛋白和丝束蛋白。^[9]骨骼肌、心脏和平滑肌亚型定位于Z盘和类似的致密体，它们有助于锚定肌原纤维肌动蛋白丝。α-肌动蛋白2已被证明与KCNA5、^[11]^[12]DLG1、^[11]DISC1、^[13]MYOZ1、^[14]GRIN2B、^[15]ADAM12、^[16]ACTN3、^[17]MYPN、^[18]PDLIM3、^[19]PKN、^[20]MYOT、^[21]TTN、^[22]NMDAR、^[23]SYNPO2、^[24]LDB3、^[25]和MYOZ1^[14]产生相互作用。

功能

α-辅肌动蛋白2的主要功能是在Z盘上交联丝状肌动蛋白分子和来自相邻肌小节的肌联蛋白分子，该功能受磷脂调节。^[26]^[27]从汉普顿等人的研究中可以清楚地看出，这种交联可以呈现多种构象，偏好60°和120°的角度。^[28]α-辅肌动蛋白2还在Z盘上的对接信号分子中发挥作用，另外的研究还表明α-辅肌动蛋白2与心脏离子通道的结合有关，尤其是K_v1.5。^[11]

临床意义

ACTN2的突变与肥厚型心肌病、^[29]扩张型心肌病和心内膜弹力纤维增生症有关。^[30]α-辅肌动蛋白2的不同功能反映在携带ACTN2突变的患者的不同临床表现中。^[31]

参考资料

^ 與Α-辅肌动蛋白2相關的疾病；在維基數據上查看/編輯參考.
^ ^2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000077522 - Ensembl, May 2017
^ ^3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000052374 - Ensembl, May 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.
^ Entrez Gene: ACTN2 actinin, alpha 2. [2023-03-10]. （原始内容存档于2010-03-05）.
^ Protein Information – Basic Information: Protein COPaKB ID: P35609. Cardiac Organellar Protein Atlas Knowledgebase. [2015-04-13]. （原始内容存档于2015-04-13）.
^ 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. Integration of cardiac proteome biology and medicine by a specialized knowledgebase. Circulation Research. October 2013, 113 (9): 1043–53. PMC 4076475 . PMID 23965338. doi:10.1161/CIRCRESAHA.113.301151.
^ ^9.0 ^9.1 Luther PK. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. Journal of Muscle Research and Cell Motility. 2009, 30 (5–6): 171–85. PMC 2799012 . PMID 19830582. doi:10.1007/s10974-009-9189-6.
^ Ribeiro Ede A, Pinotsis N, Ghisleni A, Salmazo A, Konarev PV, Kostan J, Sjöblom B, Schreiner C, Polyansky AA, Gkougkoulia EA, Holt MR, Aachmann FL, Zagrović B, Bordignon E, Pirker KF, Svergun DI, Gautel M, Djinović-Carugo K. The structure and regulation of human muscle α-actinin. Cell. December 2014, 159 (6): 1447–60. PMC 4259493 . PMID 25433700. doi:10.1016/j.cell.2014.10.056.
^ ^11.0 ^11.1 ^11.2 Eldstrom J, Choi WS, Steele DF, Fedida D. SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism. FEBS Letters. July 2003, 547 (1–3): 205–11. PMID 12860415. doi:10.1016/S0014-5793(03)00668-9 .
^ Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D. alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Letters. May 2000, 473 (2): 188–94. PMID 10812072. doi:10.1016/S0014-5793(00)01521-0 .
^ Morris JA, Kandpal G, Ma L, Austin CP. DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Human Molecular Genetics. July 2003, 12 (13): 1591–608. PMID 12812986. doi:10.1093/hmg/ddg162 .
^ ^14.0 ^14.1 Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. The Journal of Biological Chemistry. December 2000, 275 (52): 41234–42. PMID 10984498. doi:10.1074/jbc.M007493200 .
^ Wyszynski M, Lin J, Rao A, Nigh E, Beggs AH, Craig AM, Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature. January 1997, 385 (6615): 439–42. PMID 9009191. S2CID 4266742. doi:10.1038/385439a0.
^ Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E. Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion. The Journal of Biological Chemistry. May 2000, 275 (18): 13933–9. PMID 10788519. doi:10.1074/jbc.275.18.13933 .
^ Chan Y, Tong HQ, Beggs AH, Kunkel LM. Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo. Biochemical and Biophysical Research Communications. July 1998, 248 (1): 134–9. PMID 9675099. doi:10.1006/bbrc.1998.8920.
^ Bang ML, Mudry RE, McElhinny AS, Trombitás K, Geach AJ, Yamasaki R, Sorimachi H, Granzier H, Gregorio CC, Labeit S. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. The Journal of Cell Biology. April 2001, 153 (2): 413–27. PMC 2169455 . PMID 11309420. doi:10.1083/jcb.153.2.413.
^ Pomiès P, Macalma T, Beckerle MC. Purification and characterization of an alpha-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation. The Journal of Biological Chemistry. October 1999, 274 (41): 29242–50. PMID 10506181. doi:10.1074/jbc.274.41.29242 .
^ Mukai H, Toshimori M, Shibata H, Takanaga H, Kitagawa M, Miyahara M, Shimakawa M, Ono Y. Interaction of PKN with alpha-actinin. The Journal of Biological Chemistry. February 1997, 272 (8): 4740–6. PMID 9030526. doi:10.1074/jbc.272.8.4740 .
^ Salmikangas P, Mykkänen OM, Grönholm M, Heiska L, Kere J, Carpén O. Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy. Human Molecular Genetics. July 1999, 8 (7): 1329–36. PMID 10369880. doi:10.1093/hmg/8.7.1329.
^ Young P, Ferguson C, Bañuelos S, Gautel M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. The EMBO Journal. March 1998, 17 (6): 1614–24. PMC 1170509 . PMID 9501083. doi:10.1093/emboj/17.6.1614.
^ Chunn CJ, Starr PR, Gilbert DN. Neutrophil toxicity of amphotericin B. Antimicrobial Agents and Chemotherapy. August 1977, 12 (2): 226–30. PMC 429889 . PMID 900919. doi:10.1128/aac.12.2.226.
^ Linnemann A, van der Ven PF, Vakeel P, Albinus B, Simonis D, Bendas G, Schenk JA, Micheel B, Kley RA, Fürst DO. The sarcomeric Z-disc component myopodin is a multiadapter protein that interacts with filamin and alpha-actinin. European Journal of Cell Biology. September 2010, 89 (9): 681–92. PMID 20554076. doi:10.1016/j.ejcb.2010.04.004.
^ Jani K, Schöck F. Zasp is required for the assembly of functional integrin adhesion sites. The Journal of Cell Biology. December 2007, 179 (7): 1583–97. PMC 2373490 . PMID 18166658. doi:10.1083/jcb.200707045.
^ Young P, Gautel M. The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism. The EMBO Journal. December 2000, 19 (23): 6331–40. PMC 305858 . PMID 11101506. doi:10.1093/emboj/19.23.6331.
^ Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T. Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function. Nature. September 1992, 359 (6391): 150–2. PMID 1326084. S2CID 4372960. doi:10.1038/359150a0.
^ Hampton CM, Taylor DW, Taylor KA. Novel structures for alpha-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton. Journal of Molecular Biology. April 2007, 368 (1): 92–104. PMC 1919418 . PMID 17331538. doi:10.1016/j.jmb.2007.01.071.
^ Chiu C, Bagnall RD, Ingles J, Yeates L, Kennerson M, Donald JA, Jormakka M, Lind JM, Semsarian C. Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis. Journal of the American College of Cardiology. March 2010, 55 (11): 1127–35. PMID 20022194. doi:10.1016/j.jacc.2009.11.016 .
^ Mohapatra B, Jimenez S, Lin JH, Bowles KR, Coveler KJ, Marx JG, Chrisco MA, Murphy RT, Lurie PR, Schwartz RJ, Elliott PM, Vatta M, McKenna W, Towbin JA, Bowles NE. Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Molecular Genetics and Metabolism. 2003, 80 (1–2): 207–15. PMID 14567970. doi:10.1016/s1096-7192(03)00142-2.
^ Bagnall RD, Molloy LK, Kalman JM, Semsarian C. Exome sequencing identifies a mutation in the ACTN2 gene in a family with idiopathic ventricular fibrillation, left ventricular noncompaction, and sudden death. BMC Medical Genetics. September 2014, 15 (1): 99. PMC 4355500 . PMID 25224718. doi:10.1186/s12881-014-0099-0.

延申阅读

Faulkner G, Lanfranchi G, Valle G. Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life. May 2001, 51 (5): 275–82. PMID 11699871. doi:10.1080/152165401317190761 .
Beggs AH, Byers TJ, Knoll JH, Boyce FM, Bruns GA, Kunkel LM. Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11. The Journal of Biological Chemistry. May 1992, 267 (13): 9281–8. PMID 1339456. doi:10.1016/S0021-9258(19)50420-3 .
Beggs AH, Phillips HA, Kozman H, Mulley JC, Wilton SD, Kunkel LM, Laing NG. A (CA)n repeat polymorphism for the human skeletal muscle alpha-actinin gene ACTN2 and its localization on the linkage map of chromosome 1. Genomics. August 1992, 13 (4): 1314–5. PMID 1505962. doi:10.1016/0888-7543(92)90054-V.
Yürüker B, Niggli V. Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. Journal of Cell Science. February 1992, 101 (2): 403–14. PMID 1629252. doi:10.1242/jcs.101.2.403.
Pavalko FM, LaRoche SM. Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. Journal of Immunology. October 1993, 151 (7): 3795–807. PMID 8104223.
Yoshida M, Westlin WF, Wang N, Ingber DE, Rosenzweig A, Resnick N, Gimbrone MA. Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton. The Journal of Cell Biology. April 1996, 133 (2): 445–55. PMC 2120789 . PMID 8609175. doi:10.1083/jcb.133.2.445.
Wyszynski M, Lin J, Rao A, Nigh E, Beggs AH, Craig AM, Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature. January 1997, 385 (6615): 439–42. PMID 9009191. S2CID 4266742. doi:10.1038/385439a0.
Mukai H, Toshimori M, Shibata H, Takanaga H, Kitagawa M, Miyahara M, Shimakawa M, Ono Y. Interaction of PKN with alpha-actinin. The Journal of Biological Chemistry. February 1997, 272 (8): 4740–6. PMID 9030526. doi:10.1074/jbc.272.8.4740 .
Young P, Ferguson C, Bañuelos S, Gautel M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. The EMBO Journal. March 1998, 17 (6): 1614–24. PMC 1170509 . PMID 9501083. doi:10.1093/emboj/17.6.1614.
Zhang S, Ehlers MD, Bernhardt JP, Su CT, Huganir RL. Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron. August 1998, 21 (2): 443–53. PMID 9728925. S2CID 18234477. doi:10.1016/S0896-6273(00)80553-X .
Krupp JJ, Vissel B, Thomas CG, Heinemann SF, Westbrook GL. Interactions of calmodulin and alpha-actinin with the NR1 subunit modulate Ca2+-dependent inactivation of NMDA receptors. The Journal of Neuroscience. February 1999, 19 (4): 1165–78. PMC 6786025 . PMID 9952395. doi:10.1523/JNEUROSCI.19-04-01165.1999 .
Zhou Q, Ruiz-Lozano P, Martone ME, Chen J. Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C. The Journal of Biological Chemistry. July 1999, 274 (28): 19807–13. PMID 10391924. doi:10.1074/jbc.274.28.19807 .
Faulkner G, Pallavicini A, Formentin E, Comelli A, Ievolella C, Trevisan S, Bortoletto G, Scannapieco P, Salamon M, Mouly V, Valle G, Lanfranchi G. ZASP: a new Z-band alternatively spliced PDZ-motif protein. The Journal of Cell Biology. July 1999, 146 (2): 465–75. PMC 3206570 . PMID 10427098. doi:10.1083/jcb.146.2.465.
Tiso N, Majetti M, Stanchi F, Rampazzo A, Zimbello R, Nava A, Danieli GA. Fine mapping and genomic structure of ACTN2, the human gene coding for the sarcomeric isoform of alpha-actinin-2, expressed in skeletal and cardiac muscle. Biochemical and Biophysical Research Communications. November 1999, 265 (1): 256–9. PMID 10548523. doi:10.1006/bbrc.1999.1661.
Nikolopoulos SN, Spengler BA, Kisselbach K, Evans AE, Biedler JL, Ross RA. The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells. Oncogene. January 2000, 19 (3): 380–6. PMID 10656685. doi:10.1038/sj.onc.1203310 .
Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E. Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion. The Journal of Biological Chemistry. May 2000, 275 (18): 13933–9. PMID 10788519. doi:10.1074/jbc.275.18.13933 .
Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D. alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Letters. May 2000, 473 (2): 188–94. PMID 10812072. doi:10.1016/S0014-5793(00)01521-0 .
Kotaka M, Kostin S, Ngai S, Chan K, Lau Y, Lee SM, Li H, Ng EK, Schaper J, Tsui SK, Fung K, Lee C, Waye MM. Interaction of hCLIM1, an enigma family protein, with alpha-actinin 2. Journal of Cellular Biochemistry. June 2000, 78 (4): 558–65. PMID 10861853. S2CID 84122657. doi:10.1002/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-I.
Parast MM, Otey CA. Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. The Journal of Cell Biology. August 2000, 150 (3): 643–56. PMC 2175193 . PMID 10931874. doi:10.1083/jcb.150.3.643.
Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. The Journal of Biological Chemistry. December 2000, 275 (52): 41234–42. PMID 10984498. doi:10.1074/jbc.M007493200 .

外部链接

Mass spectrometry characterization of human ACTN2 at COPaKB
GeneReviews/NIH/NCBI/UW entry on Familial Hypertrophic Cardiomyopathy Overview （页面存档备份，存于互联网档案馆）
Human ACTN2 genome location and ACTN2 gene details page in the UCSC Genome Browser（英语：UCSC Genome Browser）.

[1] 與Α-辅肌动蛋白2相關的疾病；在維基數據上查看/編輯參考.

[refGRCh38Ensembl-2] 2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000077522 - Ensembl, May 2017

[refGRCm38Ensembl-3] 3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000052374 - Ensembl, May 2017

[4] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-6] Entrez Gene: ACTN2 actinin, alpha 2. [2023-03-10]. （原始内容存档于2010-03-05）.

[7] Protein Information – Basic Information: Protein COPaKB ID: P35609. Cardiac Organellar Protein Atlas Knowledgebase. [2015-04-13]. （原始内容存档于2015-04-13）.

[cite_PMID_|_23965338-8] 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. Integration of cardiac proteome biology and medicine by a specialized knowledgebase. Circulation Research. October 2013, 113 (9): 1043–53. PMC 4076475 . PMID 23965338. doi:10.1161/CIRCRESAHA.113.301151.

[cite_PMID_|_19830582-9] 9.0 ^9.1 Luther PK. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. Journal of Muscle Research and Cell Motility. 2009, 30 (5–6): 171–85. PMC 2799012 . PMID 19830582. doi:10.1007/s10974-009-9189-6.

[10] Ribeiro Ede A, Pinotsis N, Ghisleni A, Salmazo A, Konarev PV, Kostan J, Sjöblom B, Schreiner C, Polyansky AA, Gkougkoulia EA, Holt MR, Aachmann FL, Zagrović B, Bordignon E, Pirker KF, Svergun DI, Gautel M, Djinović-Carugo K. The structure and regulation of human muscle α-actinin. Cell. December 2014, 159 (6): 1447–60. PMC 4259493 . PMID 25433700. doi:10.1016/j.cell.2014.10.056.

[pmid12860415-11] 11.0 ^11.1 ^11.2 Eldstrom J, Choi WS, Steele DF, Fedida D. SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism. FEBS Letters. July 2003, 547 (1–3): 205–11. PMID 12860415. doi:10.1016/S0014-5793(03)00668-9 .

[pmid10812072-12] Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D. alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Letters. May 2000, 473 (2): 188–94. PMID 10812072. doi:10.1016/S0014-5793(00)01521-0 .

[pmid12812986-13] Morris JA, Kandpal G, Ma L, Austin CP. DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Human Molecular Genetics. July 2003, 12 (13): 1591–608. PMID 12812986. doi:10.1093/hmg/ddg162 .

[pmid10984498-14] 14.0 ^14.1 Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. The Journal of Biological Chemistry. December 2000, 275 (52): 41234–42. PMID 10984498. doi:10.1074/jbc.M007493200 .

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