骨骼肌肌动蛋白α1

骨骼肌肌动蛋白α1
已知的结构
PDB	直系同源搜索: PDBe RCSB
PDBID列表
	1T44
识别号
别名	ACTA1；, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle
外部ID	OMIM：102610 MGI：87909 HomoloGene：121702 GeneCards：ACTA1
相关疾病
	congenital myopathy with excess of thin filaments
基因位置（人类）
染色体	1号染色体
终止	229,434,104 bp
基因位置（小鼠）
染色体	小鼠19号染色体
终止	34,232,990 bp
RNA表达模式
	查阅更多表达数据
基因本体
分子功能	• 核苷酸结合; • myosin binding; • ADP binding; • structural constituent of cytoskeleton; • 血浆蛋白结合; • ATP结合;
细胞组分	• 细胞质; • cell body; • 细胞质基质; • blood microparticle; • 丝状伪足; • 肌节; • striated muscle thin filament; • 应力纤维; • 细胞外液; • 微丝; • actin cytoskeleton; • 外排体; • 细胞骨架; • 板状伪足;
生物学过程	• 肌肉收缩; • response to steroid hormone; • skeletal muscle fiber adaptation; • response to mechanical stimulus; • skeletal muscle thin filament assembly; • response to lithium ion; • 增殖; • positive regulation of gene expression; • muscle filament sliding; • mesenchyme migration; • response to extracellular stimulus; • skeletal muscle fiber development;
	Sources:Amigo / QuickGO
直系同源
	58
	11475
	ENSG00000143632
	ENSMUSG00000035783
	P68133
	P62737
	NM_001100
	NM_007392
	NP_001091
	NP_031418
	维基数据
查看/编辑人类	查看/编辑小鼠

骨骼肌肌动蛋白α1（英语：Skeletal muscle, actin alpha 1）是一种在人类中由ACTA1基因编码的蛋白质。^[6]^[7]

在骨骼肌中表达的肌动蛋白α1是已鉴定的六种不同肌动蛋白亚型之一。肌动蛋白是高度保守的蛋白质，它们参与细胞运动、结构和完整性。α肌动蛋白是收缩装置的主要成分。^[8]

骨骼肌肌动蛋白基因表达

骨骼α肌动蛋白的表达是由已知会导致肌肉形成的刺激和条件诱导的。^[9]这种情况导致定型细胞（卫星细胞）融合到肌管中，形成肌纤维。骨骼肌动蛋白本身在表达时会引起其他几种“生肌基因”的表达，这些基因对肌肉形成至关重要。^[10]激活骨骼肌动蛋白基因表达的一个关键转录因子是血清反应因子，一种结合肌动蛋白基因启动子DNA上特定位点的蛋白质。^[11]血清反应因子可以将许多其他蛋白质带到骨骼肌动蛋白的启动子，例如雄激素受体，从而有助于通过雄激素（通常称为合成代谢）类固醇诱导骨骼肌动蛋白基因表达。^[12]

相互作用

肌动蛋白α1已被证明与TMSB4X、^[13]^[14]MIB2^[15]和PRKCE产生相互作用。^[16]

参见

参考资料

^ 與骨骼肌肌动蛋白α1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: ENSG00000143632 - Ensembl, May 2017
^ ^3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000035783 - 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.
^ Mogensen J, Kruse TA, Børglum AD. Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping. Cytogenetics and Cell Genetics. March 1999, 83 (3–4): 224–5. PMID 10072583. S2CID 84202330. doi:10.1159/000015184.
^ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L. Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. Molecular and Cellular Biology. May 1983, 3 (5): 787–95. PMC 368601  . PMID 6865942. doi:10.1128/mcb.3.5.787.
^ Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle. [2023-03-08]. （原始内容存档于2010-03-07）.
^ Bandman E. Contractile protein isoforms in muscle development. Developmental Biology. December 1992, 154 (2): 273–83. PMID 1358730. doi:10.1016/0012-1606(92)90067-Q.
^ Gunning PW, Ferguson V, Brennan KJ, Hardeman EC. Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle. Journal of Cell Science. February 2001, 114 (Pt 3): 513–24. PMID 11171321. doi:10.1242/jcs.114.3.513.
^ Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ. Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets. Molecular and Cellular Biology. July 1999, 19 (7): 4582–91. PMC 84256  . PMID 10373507. doi:10.1128/mcb.19.7.4582.
^ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ. Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene. The Journal of Biological Chemistry. March 2005, 280 (9): 7786–92. PMID 15623502. doi:10.1074/jbc.M413992200  .
^ Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG. Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin. Journal of Molecular Biology. January 2002, 315 (4): 613–25. PMID 11812134. doi:10.1006/jmbi.2001.5281.
^ Safer D, Sosnick TR, Elzinga M. Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry. May 1997, 36 (19): 5806–16. PMID 9153421. doi:10.1021/bi970185v.
^ Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y. Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma. The American Journal of Pathology. October 2003, 163 (4): 1395–404. PMC 1868282  . PMID 14507647. doi:10.1016/S0002-9440(10)63497-9.
^ England K, Ashford D, Kidd D, Rumsby M. PKC epsilon is associated with myosin IIA and actin in fibroblasts. Cellular Signalling. June 2002, 14 (6): 529–36. PMID 11897493. doi:10.1016/S0898-6568(01)00277-7.

延申阅读

Snásel J, Pichová I. The cleavage of host cell proteins by HIV-1 protease. Folia Biologica. 1997, 42 (5): 227–30. PMID 8997639. S2CID 7617882. doi:10.1007/BF02818986.
Di Fiore PP, Scita G. Eps8 in the midst of GTPases. The International Journal of Biochemistry & Cell Biology. October 2002, 34 (10): 1178–83. PMID 12127568. doi:10.1016/S1357-2725(02)00064-X.
Ogawa H, Shiraki H, Matsuda Y, Nakagawa H. Interaction of adenylosuccinate synthetase with F-actin. European Journal of Biochemistry. April 1978, 85 (2): 331–7. PMID 648524. doi:10.1111/j.1432-1033.1978.tb12243.x.
den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J. The EGF receptor is an actin-binding protein. The Journal of Cell Biology. October 1992, 119 (2): 349–55. PMC 2289650  . PMID 1383230. doi:10.1083/jcb.119.2.349.
Adams LD, Tomasselli AG, Robbins P, Moss B, Heinrikson RL. HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. AIDS Research and Human Retroviruses. February 1992, 8 (2): 291–5 [2023-03-08]. PMID 1540415. doi:10.1089/aid.1992.8.291. （原始内容存档于2021-03-11）.
Levine BA, Moir AJ, Patchell VB, Perry SV. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Letters. February 1992, 298 (1): 44–8. PMID 1544421. doi:10.1016/0014-5793(92)80019-D  .
Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J. Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells. Journal of Cell Science. November 1991,. 100 ( Pt 3) (3): 491–9. PMID 1808202. doi:10.1242/jcs.100.3.491  .
Tomasselli AG, Hui JO, Adams L, Chosay J, Lowery D, Greenberg B, Yem A, Deibel MR, Zürcher-Neely H, Heinrikson RL. Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. The Journal of Biological Chemistry. August 1991, 266 (22): 14548–53. PMID 1907279. doi:10.1016/S0021-9258(18)98721-1  .
Shoeman RL, Kesselmier C, Mothes E, Höner B, Traub P. Non-viral cellular substrates for human immunodeficiency virus type 1 protease. FEBS Letters. January 1991, 278 (2): 199–203. PMID 1991513. doi:10.1016/0014-5793(91)80116-K  .
Winder SJ, Walsh MP. Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. The Journal of Biological Chemistry. June 1990, 265 (17): 10148–55. PMID 2161834. doi:10.1016/S0021-9258(19)38792-7  .
Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. Atomic structure of the actin:DNase I complex. Nature. September 1990, 347 (6288): 37–44. Bibcode:1990Natur.347...37K. PMID 2395459. S2CID 925337. doi:10.1038/347037a0.
Takahashi K, Hiwada K, Kokubu T. Vascular smooth muscle calponin. A novel troponin T-like protein. Hypertension. June 1988, 11 (6 Pt 2): 620–6. PMID 2455687. doi:10.1161/01.hyp.11.6.620  .
Taylor A, Erba HP, Muscat GE, Kedes L. Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains. Genomics. November 1988, 3 (4): 323–36. PMID 2907503. doi:10.1016/0888-7543(88)90123-1.
Shen BW, Josephs R, Steck TL. Ultrastructure of the intact skeleton of the human erythrocyte membrane. The Journal of Cell Biology. March 1986, 102 (3): 997–1006. PMC 2114132  . PMID 2936753. doi:10.1083/jcb.102.3.997.
Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. The Journal of Cell Biology. January 1987, 104 (1): 29–40. PMC 2117036  . PMID 3793760. doi:10.1083/jcb.104.1.29.
Kedes L, Ng SY, Lin CS, Gunning P, Eddy R, Shows T, Leavitt J. The human beta-actin multigene family. Transactions of the Association of American Physicians. 1986, 98: 42–6. PMID 3842206.
Hanauer A, Levin M, Heilig R, Daegelen D, Kahn A, Mandel JL. Isolation and characterization of cDNA clones for human skeletal muscle alpha actin. Nucleic Acids Research. June 1983, 11 (11): 3503–16. PMC 325982  . PMID 6190133. doi:10.1093/nar/11.11.3503.
Bretscher A, Weber K. Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Cell. July 1980, 20 (3): 839–47. PMID 6893424. S2CID 568395. doi:10.1016/0092-8674(80)90330-X.

外部链接

GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy （页面存档备份，存于互联网档案馆）
Human ACTA1 genome location and ACTA1 gene details page in the UCSC Genome Browser（英语：UCSC Genome Browser）.

[1] 與骨骼肌肌动蛋白α1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: ENSG00000143632 - Ensembl, May 2017

[refGRCm38Ensembl-3] 3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000035783 - 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.

[pmid10072583-6] Mogensen J, Kruse TA, Børglum AD. Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping. Cytogenetics and Cell Genetics. March 1999, 83 (3–4): 224–5. PMID 10072583. S2CID 84202330. doi:10.1159/000015184.

[pmid6865942-7] Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L. Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. Molecular and Cellular Biology. May 1983, 3 (5): 787–95. PMC 368601  . PMID 6865942. doi:10.1128/mcb.3.5.787.

[entrez-8] Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle. [2023-03-08]. （原始内容存档于2010-03-07）.

[9] Bandman E. Contractile protein isoforms in muscle development. Developmental Biology. December 1992, 154 (2): 273–83. PMID 1358730. doi:10.1016/0012-1606(92)90067-Q.

[10] Gunning PW, Ferguson V, Brennan KJ, Hardeman EC. Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle. Journal of Cell Science. February 2001, 114 (Pt 3): 513–24. PMID 11171321. doi:10.1242/jcs.114.3.513.

[11] Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ. Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets. Molecular and Cellular Biology. July 1999, 19 (7): 4582–91. PMC 84256  . PMID 10373507. doi:10.1128/mcb.19.7.4582.

[12] Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ. Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene. The Journal of Biological Chemistry. March 2005, 280 (9): 7786–92. PMID 15623502. doi:10.1074/jbc.M413992200  .

[pmid11812134-13] Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG. Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin. Journal of Molecular Biology. January 2002, 315 (4): 613–25. PMID 11812134. doi:10.1006/jmbi.2001.5281.

[pmid9153421-14] Safer D, Sosnick TR, Elzinga M. Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry. May 1997, 36 (19): 5806–16. PMID 9153421. doi:10.1021/bi970185v.

[pmid14507647-15] Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y. Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma. The American Journal of Pathology. October 2003, 163 (4): 1395–404. PMC 1868282  . PMID 14507647. doi:10.1016/S0002-9440(10)63497-9.

[pmid11897493-16] England K, Ashford D, Kidd D, Rumsby M. PKC epsilon is associated with myosin IIA and actin in fibroblasts. Cellular Signalling. June 2002, 14 (6): 529–36. PMID 11897493. doi:10.1016/S0898-6568(01)00277-7.

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