利用者:空色水色/Α-アクチニン1

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α-アクチニン1（α-actinin-1）とは、ヒトのACTN1遺伝子にコードされたタンパク質である。^[1]

機能

α-アクチニンは、細胞骨格タンパク質のグループであるスペクトリンスーパーファミリーに属する。アルファアクチニンはアクチン結合タンパク質であり、異なる細胞型において複数の役割を示す。非筋細胞において、細胞骨格アイソフォームは、膜へのアクチンの結合に関与するマイクロフィラメント束および接着結合で見出される。一方で、骨格、心臓、および平滑筋でのアイソフォームは、Z-discおよび類似の高密度体に局在し、筋原線維アクチンフィラメントの固定に役立つ。α-アクチニン1の遺伝子は、非筋肉の細胞骨格α-アクチニンアイソフォームをコードし、類似の構造の赤血球β-スペクトリン遺伝子と同じ部位に位置する。^[2]

相互作用

α-アクチニン1は以下の生体物質と相互作用する:

CDK5R1^[3]
CDK5R2
XVII型コラーゲン α1^[4]
GIPC1^[5]
PDLIM1^[6]^[7]
タンパク質キナーゼN1^[8]
SSX2IP^[9]
ザイキシン^[10]^[11]
PTPRT(PTPrho)^[12]

References

^ “Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene”. Am J Hum Genet 47 (1): 62–72. (Jul 1990). PMC 1683765. PMID 2349951.
^ “Entrez Gene: ACTN1 actinin, alpha 1”. Template:Cite webの呼び出しエラー：引数 accessdate は必須です。
^ “The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner”. J. Neurosci. 22 (18): 7879–91. (September 2002). PMID 12223541.
^ “Interactions of a hemidesmosome component and actinin family members”. J. Cell Sci. 114 (Pt 23): 4197–206. (December 2001). PMID 11739652.
^ “Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton”. Mol. Biol. Cell 10 (4): 819–32. (April 1999). doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
^ “CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4”. J. Biol. Chem. 275 (15): 11100–5. (April 2000). doi:10.1074/jbc.275.15.11100. PMID 10753915.
^ “Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells”. Blood 96 (13): 4236–45. (December 2000). PMID 11110697.
^ “Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex”. Biochemistry 41 (4): 1100–8. (January 2002). doi:10.1021/bi0156005. PMID 11802708.
^ “ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions”. J. Biol. Chem. 278 (6): 4103–11. (February 2003). doi:10.1074/jbc.M209832200. PMID 12446711.
^ “An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment”. J. Biol. Chem. 274 (19): 13410–8. (May 1999). doi:10.1074/jbc.274.19.13410. PMID 10224105.
^ “Analysis of the alpha-actinin/zyxin interaction”. J. Biol. Chem. 276 (36): 33328–35. (September 2001). doi:10.1074/jbc.M100789200. PMID 11423549.
^ “Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).”. Brain Res 1116 (1): 50–7. (2006). doi:10.1016/j.brainres.2006.07.122. PMID 16973135.

[pmid2349951-1] “Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene”. Am J Hum Genet 47 (1): 62–72. (Jul 1990). PMC 1683765. PMID 2349951.

[2] “Entrez Gene: ACTN1 actinin, alpha 1”. Template:Cite webの呼び出しエラー：引数 accessdate は必須です。

[pmid12223541-3] “The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner”. J. Neurosci. 22 (18): 7879–91. (September 2002). PMID 12223541.

[pmid11739652-4] “Interactions of a hemidesmosome component and actinin family members”. J. Cell Sci. 114 (Pt 23): 4197–206. (December 2001). PMID 11739652.

[pmid10198040-5] “Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton”. Mol. Biol. Cell 10 (4): 819–32. (April 1999). doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.

[pmid10753915-6] “CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4”. J. Biol. Chem. 275 (15): 11100–5. (April 2000). doi:10.1074/jbc.275.15.11100. PMID 10753915.

[pmid11110697-7] “Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells”. Blood 96 (13): 4236–45. (December 2000). PMID 11110697.

[pmid11802708-8] “Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex”. Biochemistry 41 (4): 1100–8. (January 2002). doi:10.1021/bi0156005. PMID 11802708.

[pmid12446711-9] “ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions”. J. Biol. Chem. 278 (6): 4103–11. (February 2003). doi:10.1074/jbc.M209832200. PMID 12446711.

[pmid10224105-10] “An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment”. J. Biol. Chem. 274 (19): 13410–8. (May 1999). doi:10.1074/jbc.274.19.13410. PMID 10224105.

[pmid11423549-11] “Analysis of the alpha-actinin/zyxin interaction”. J. Biol. Chem. 276 (36): 33328–35. (September 2001). doi:10.1074/jbc.M100789200. PMID 11423549.

[pmid16973135-12] “Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).”. Brain Res 1116 (1): 50–7. (2006). doi:10.1016/j.brainres.2006.07.122. PMID 16973135.

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