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Polo-like kinase 2 (PLK2) phosphorylates α-synuclein at Serine 129 in central nervous system

หน่วยงาน Central Queensland University, Australia

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ชื่อเรื่อง : Polo-like kinase 2 (PLK2) phosphorylates α-synuclein at Serine 129 in central nervous system
นักวิจัย : Inglis, Kelly J. , Chereau, David. , Wright, Sarah. , Chian, David. , Santiago, Pamela. , Soriano, Ferdie. , Ramos, Carla. , Powell, Kyle. , Goldstein, Jason M. , Babcock, Michael. , Yednock, Ted. , Bard, Frederique. , Brigham, Elizabeth F. , Basi, Gurigbal S. , Sham, Hing. , Chilcote, Tamie J. , McConlogue, Lisa. , Griswold-Prenner, Irene. , Anderson, Johan P. , Chiou, San-San. , Schobel, Susanne. , Frigon, Normand L. , Yu, Mei. , Caccavello, Russell J. , Nelson, S. , Motter, Ruth.
คำค้น : Strategic basic research. , 110999 Neurosciences not elsewhere classified. , Neurological diseases -- Parkinson disease -- Dementia -- Lewdy bodies , Journal Article. Refereed, Scholarly Journal
หน่วยงาน : Central Queensland University, Australia
ผู้ร่วมงาน : -
ปีพิมพ์ : 2552
อ้างอิง : http://hdl.cqu.edu.au/10018/1016327
ที่มา : Inglis, KJ, Chereau, D, Brigham, EF, Chiou, S, Schöbel, S, Frigon, NL, Yu, M, Caccavello, RJ, Nelson, S, Motter, R, Wright, S, Chian, D, Santiago, P, Soriano, F, Ramos, C, Powell, K, Goldstein, JM, Babcock, M, Yednock, T, Bard, F, Basi, GS, Sham, H, Chilcote, TJ, McConlogue, L, Griswold-Prenner, I & Anderson, JP 2009, 'Polo-like Kinase 2 (PLK2) Phosphorylates α-Synuclein at Serine 129 in Central Nervous System', Journal of Biological Chemistry, vol. 284, no. 5, pp. 2598-2602, http://dx.doi.org/10.1074/jbc.C800206200
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Journal of biological chemistry. USA : American Society for Biochemistry and Molecular Biology, 2009. Vol. 284, no. 5 (January 2009), p. 2598-2602 5 pages Refereed 0021-9258 1083-351X (online) , ACQUIRE [electronic resource] : Central Queensland University Institutional Repository.
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Several neurological diseases, including Parkinson disease and dementia with Lewy bodies, are characterized by the accumulation of α-synuclein phosphorylated at Ser-129 (p-Ser-129). The kinase or kinases responsible for this phosphorylation have been the subject of intense investigation. Here we submit evidence that polo-likekinase 2 (PLK2, also known as serum-inducible kinase or SNK) is a principle contributor to α-synuclein phosphorylation at Ser-129 in neurons. PLK2 directly phosphorylates α-synuclein at Ser-129 in an in vitro biochemical assay. Inhibitors of PLK kinases inhibited α-synuclein phosphorylation both in primary cortical cell cultures and in mouse brain in vivo. Finally, specific knockdown of PLK2 expression by transduction with short hairpin RNA constructs or by knock-out of the plk2 gene reduced p-Ser-129 levels. These results indicate that PLK2 plays a critical role in α-synuclein phosphorylation in central nervous system.

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