ACTA1

ACTA1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1T44
Identifikatori
Aliasi	ACTA1
Vanjski ID-jevi	OMIM: 102610 MGI: 87902 HomoloGene: 121702 GeneCards: ACTA1
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	229,434,104 bp
Lokacija gena (miš)
Hrom.	Hromosom 8 (miš)
Kraj	124,621,490 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• nucleotide binding; • myosin binding; • ADP binding; • structural constituent of cytoskeleton; • GO:0001948, GO:0016582 vezivanje za proteine; • ATP binding;
Ćelijska komponenta	• citoplazma; • cell body; • citosol; • blood microparticle; • Filopodija; • Sarkomera; • striated muscle thin filament; • stress fiber; • Vanćelijska tečnost; • Mikronit; • actin cytoskeleton; • Egzosom; • citoskelet; • lamellipodium;
Biološki proces	• Mišićna kontrakcija; • response to steroid hormone; • skeletal muscle fiber adaptation; • response to mechanical stimulus; • skeletal muscle thin filament assembly; • response to lithium ion; • Ćelijski rast; • GO:1901313 positive regulation of gene expression; • muscle filament sliding; • mesenchyme migration; • response to extracellular stimulus; • skeletal muscle fiber development;
	Izvori:Amigo / QuickGO
Ortolozi
	58
	11459
	ENSG00000143632
	ENSMUSG00000031972
	P68133
	P68134
	NM_001100
	NM_001272041; NM_009606
	NP_001091
	NP_001258970; NP_033736
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Aktin alfa skeletnih mišića je protein koji je kod ljudi kodiran genom ACTA.^[5]^[6]

Aktin alfa 1 koji se ispoljava u skeletnim mišićima jedna je od šest različitih identificiranih izoformi aktina. Aktini su visoko konzervirani proteini, koji su uključeni u pokretljivost ćelija, strukturu i integritet. Alfa aktini su glavni sastojak kontraktilnog aparata.^[7]

Ekspresija aktinskog gena skeletnih mišića[uredi | uredi izvor]

Ekspresija alfa aktina u skeletnim mišićima inducirana je podražajima i stanjima za koja je poznato da uzrokuju formiranje mišića.^[8] Takvi uslovi rezultiraju fuzijom povezanih ćelija (satelitskih ćelija) u miotube, da bi se stvorila mišićna vlakna. Sam skeletni aktin, kada se eksprimira, uzrokuje ekspresiju nekoliko drugih "miogenih gena", koji su neophodni za formiranje mišića.^[9] Jedan od ključnih transkripcijski faktor€transkripcijskih faktora koji aktivira ekspresiju aktinskog gena skeletnih mišića je faktor serumskog odgovora ("SRF"), protein koji se veže na određena mjesta na promotorskoj DNK aktinskog gena.^[10] SRF može donijeti brojne druge proteine promotoru ovog aktina, kao što je androgeni receptor, i na taj način doprinijeti indukciji ekspresije gena aktina androgenima (često nazivanim "anaboličkim") steroid.^[11]

Interakcije[uredi | uredi izvor]

Pokazano je da aktin, alfa 1 ima interakcije sa TMSB4X,^[12]^[13] MIB2^[14] i PRKCE.^[15]

Također pogledajte[uredi | uredi izvor]

Aktin
ACTB

Reference[uredi | uredi izvor]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143632 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031972 - 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.
^ Mogensen J, Kruse TA, Børglum AD (mart 1999). "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. 83 (3–4): 224–5. doi:10.1159/000015184. PMID 10072583.
^ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (maj 1983). "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. 3 (5): 787–95. doi:10.1128/mcb.3.5.787. PMC 368601. PMID 6865942.
^ "Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle".
^ Bandman E (decembar 1992). "Contractile protein isoforms in muscle development". Developmental Biology. 154 (2): 273–83. doi:10.1016/0012-1606(92)90067-Q. PMID 1358730.
^ Gunning PW, Ferguson V, Brennan KJ, Hardeman EC (februar 2001). "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle". Journal of Cell Science. 114 (Pt 3): 513–24. PMID 11171321.
^ Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ (juli 1999). "Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets". Molecular and Cellular Biology. 19 (7): 4582–91. doi:10.1128/mcb.19.7.4582. PMC 84256. PMID 10373507.
^ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (mart 2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". The Journal of Biological Chemistry. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
^ Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG (januar 2002). "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. 315 (4): 613–25. doi:10.1006/jmbi.2001.5281. PMID 11812134.
^ Safer D, Sosnick TR, Elzinga M (maj 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry. 36 (19): 5806–16. doi:10.1021/bi970185v. PMID 9153421.
^ Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y (oktobar 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". The American Journal of Pathology. 163 (4): 1395–404. doi:10.1016/S0002-9440(10)63497-9. PMC 1868282. PMID 14507647.
^ England K, Ashford D, Kidd D, Rumsby M (juni 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cellular Signalling. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. PMID 11897493.

Dopunska literatura[uredi | uredi izvor]

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

Vanjski linkovi[uredi | uredi izvor]

GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy
Lokacija ljudskog genoma ACTA1 i stranica sa detaljima o genu ACTA1 u UCSC Genome Browseru.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143632 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031972 - 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.

[pmid10072583-5] Mogensen J, Kruse TA, Børglum AD (mart 1999). "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. 83 (3–4): 224–5. doi:10.1159/000015184. PMID 10072583.

[pmid6865942-6] Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (maj 1983). "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. 3 (5): 787–95. doi:10.1128/mcb.3.5.787. PMC 368601. PMID 6865942.

[entrez-7] "Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle".

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

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

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

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

[pmid11812134-12] Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG (januar 2002). "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. 315 (4): 613–25. doi:10.1006/jmbi.2001.5281. PMID 11812134.

[pmid9153421-13] Safer D, Sosnick TR, Elzinga M (maj 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry. 36 (19): 5806–16. doi:10.1021/bi970185v. PMID 9153421.

[pmid14507647-14] Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y (oktobar 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". The American Journal of Pathology. 163 (4): 1395–404. doi:10.1016/S0002-9440(10)63497-9. PMC 1868282. PMID 14507647.

[pmid11897493-15] England K, Ashford D, Kidd D, Rumsby M (juni 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cellular Signalling. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. PMID 11897493.

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