骨骼肌肌動蛋白α1

骨骼肌肌動蛋白α1
已知的結構
PDB	直系同源搜尋: PDBe RCSB
PDBID列表
	1T44
識別號
別名	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
相關疾病
	congenital myopathy with excess of thin filaments
基因位置（人類）
染色體	1號染色體
終止	229,434,104 bp
基因位置（小鼠）
染色體	小鼠19號染色體
終止	34,232,990 bp
RNA表現模式
	查閱更多表現資料
基因本體
分子功能	• 核苷酸結合; • myosin binding; • ADP binding; • structural constituent of cytoskeleton; • 血漿蛋白結合; • ATP結合;
細胞組分	• 細胞質; • cell body; • 細胞質基質; • blood microparticle; • 絲狀偽足; • 肌節; • striated muscle thin filament; • 應力纖維; • 細胞外液; • 微絲; • actin cytoskeleton; • 外排體; • 細胞骨架; • 板狀偽足;
生物學過程	• 肌肉收縮; • 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
	維基資料
檢視/編輯人類	檢視/編輯小鼠

骨骼肌肌動蛋白α1（英語：Skeletal muscle, actin alpha 1）是一種在人類中由ACTA1基因編碼的蛋白質。^[6]^[7]

在骨骼肌中表現的肌動蛋白α1是已鑑定的六種不同肌動蛋白亞型之一。肌動蛋白是高度保守的蛋白質，它們參與細胞運動、結構和完整性。α肌動蛋白是收縮裝置的主要成分。^[8]

骨骼肌肌動蛋白基因表現

骨骼α肌動蛋白的表現是由已知會導致肌肉形成的刺激和條件誘導的。^[9]這種情況導致定型細胞（衛星細胞）融合到肌管中，形成肌纖維。骨骼肌動蛋白本身在表現時會引起其他幾種「生肌基因」的表現，這些基因對肌肉形成至關重要。^[10]活化骨骼肌動蛋白基因表現的一個關鍵轉錄因子是血清反應因子，一種結合肌動蛋白基因啟動子DNA上特定位點的蛋白質。^[11]血清反應因子可以將許多其他蛋白質帶到骨骼肌動蛋白的啟動子，例如雄激素受體，從而有助於通過雄激素（通常稱為合成代謝）類固醇誘導骨骼肌動蛋白基因表現。^[12]

相互作用

肌動蛋白α1已被證明與TMSB4X、^[13]^[14]MIB2^[15]和PRKCE產生相互作用。^[16]

參見

參考資料

^ 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]. （原始內容存檔於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.

延申閱讀

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. （原始內容存檔於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.

外部連結

GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy （頁面存檔備份，存於網際網路檔案館）
Human ACTA1 genome location and ACTA1 gene details page in the UCSC Genome Browser（英語：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]. （原始內容存檔於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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