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PINK1

PTEN induced putative kinase 1

Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PARK2. Targets PARK2 to dysfunctional depolarized mitochondria through the phosphorylation of MFN2. Activates PARK2 in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PARK2 and (2) mediating phosphorylation of ubiquitin, converting PARK2 to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582).

Gene Name:	PTEN induced putative kinase 1
Family/Subfamily:	Protein Kinase , NFK
Synonyms:	PINK1, BRPK, PTEN induced putative kinase 1, PARK6, PTEN-induced putative kinase, Protein kinase BRPK
Target Sequences:	NM_032409 NP_115785.1 Q9BXM7

Publications (23)

Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. Exner N, Treske B, Paquet D, Holmstrm K, Schiesling C, Gispert S, Carballo-Carbajal I, Berg D, Hoepken HH, Gasser T, Krger R, Winklhofer KF, Vogel F, Reichert AS, Auburger G, Kahle PJ, Schmid B, Haass C. The Journal of neuroscience : the official journal of the Society for Neuroscience. 2007 27:12413-8. (WB) [PubMed:17989306]

Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. Weihofen A, Ostaszewski B, Minami Y, Selkoe DJ. Human molecular genetics. 2008 17:602-16. [PubMed:18003639]

Characterization of PINK1 processing, stability, and subcellular localization. Lin W, Kang UJ. Journal of neurochemistry. 2008 106:464-74. (WB; Human) [PubMed:18397367]

The kinase domain of mitochondrial PINK1 faces the cytoplasm. Zhou C, Huang Y, Shao Y, May J, Prou D, Perier C, Dauer W, Schon EA, Przedborski S. Proceedings of the National Academy of Sciences of the United States of America. 2008 105:12022-7. [PubMed:18687899] [PMC:PMC2575334]

PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease. Liu W, Vives-Bauza C, Acn-Perz- R, Yamamoto A, Tan Y, Li Y, Magran J, Stavarache MA, Shaffer S, Chang S, Kaplitt MG, Huang XY, Beal MF, Manfredi G, Li C. PloS one. 2009 4:e4597. [PubMed:19242547] [PMC:PMC2644779]

Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. Lutz AK, Exner N, Fett ME, Schlehe JS, Kloos K, Lmmermann K, Brunner B, Kurz-Drexler A, Vogel F, Reichert AS, Bouman L, Vogt-Weisenhorn D, Wurst W, Tatzelt J, Haass C, Winklhofer KF. The Journal of biological chemistry. 2009 284:22938-51. [PubMed:19546216] [PMC:PMC2755701]

Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1. Cui M, Tang X, Christian WV, Yoon Y, Tieu K. The Journal of biological chemistry. 2010 285:11740-52. [PubMed:20164189] [PMC:PMC2857048]

Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics. Irrcher I, Aleyasin H, Seifert EL, Hewitt SJ, Chhabra S, Phillips M, Lutz AK, Rousseaux MW, Bevilacqua L, Jahani-Asl A, Callaghan S, MacLaurin JG, Winklhofer KF, Rizzu P, Rippstein P, Kim RH, Chen CX, Fon EA, Slack RS, Harper ME, McBride HM, Mak TW, Park. Human molecular genetics. 2010 19:3734-46. (WB; Mouse) [PubMed:20639397]

Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Cui J, Yao Q, Li S, Ding X, Lu Q, Mao H, Liu L, Zheng N, Chen S, Shao F. Science (New York, N.Y.). 2010 329:1215-8. [PubMed:20688984] [PMC:PMC3031172]

The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Geisler S, Holmstrm KM, Treis A, Skujat D, Weber SS, Fiesel FC, Kahle PJ, Springer W. Autophagy. 2010 6:871-8. (WB; Human) [PubMed:20798600]

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. Meissner C, Lorenz H, Weihofen A, Selkoe DJ, Lemberg MK. Journal of neurochemistry. 2011 117:856-67. [PubMed:21426348]

Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease. Dagda RK, Gusdon AM, Pien I, Strack S, Green S, Li C, Van Houten B, Cherra SJ, Chu CT. Cell death and differentiation. 2011 18:1914-23. [PubMed:21637291] [PMC:PMC3177020]

Muscle choline kinase beta defect causes mitochondrial dysfunction and increased mitophagy. Mitsuhashi S, Hatakeyama H, Karahashi M, Koumura T, Nonaka I, Hayashi YK, Noguchi S, Sher RB, Nakagawa Y, Manfredi G, Goto Y, Cox GA, Nishino I. Human molecular genetics. 2011 20:3841-51. (ICC, IHC; Mouse) [PubMed:21750112] [PMC:PMC3168292]

Parkin-mediated protection of dopaminergic neurons in a chronic MPTP-minipump mouse model of Parkinson disease. Yasuda T, Hayakawa H, Nihira T, Ren YR, Nakata Y, Nagai M, Hattori N, Miyake K, Takada M, Shimada T, Mizuno Y, Mochizuki H. Journal of neuropathology and experimental neurology. 2011 70:686-97. (WB; Mouse) [PubMed:21760537]

PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, Gourlay R, Burchell L, Walden H, Macartney TJ, Deak M, Knebel A, Alessi DR, Muqit MM. Open biology. 2012 2:120080. (WB; Human) [PubMed:22724072] [PMC:PMC3376738]

PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Okatsu K, Oka T, Iguchi M, Imamura K, Kosako H, Tani N, Kimura M, Go E, Koyano F, Funayama M, Shiba-Fukushima K, Sato S, Shimizu H, Fukunaga Y, Taniguchi H, Komatsu M, Hattori N, Mihara K, Tanaka K, Matsuda N. Nature communications. 2012 3:1016. (ICC, WB; Mouse, Human) [PubMed:22910362] [PMC:PMC3432468]

Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5. Sekine S, Kanamaru Y, Koike M, Nishihara A, Okada M, Kinoshita H, Kamiyama M, Maruyama J, Uchiyama Y, Ishihara N, Takeda K, Ichijo H. The Journal of biological chemistry. 2012 287:34635-45. [PubMed:22915595] [PMC:PMC3464569]

The role of the mitochondrial NCX in the mechanism of neurodegeneration in Parkinson's disease. Wood-Kaczmar A, Deas E, Wood NW, Abramov AY. Advances in experimental medicine and biology. 2013 961:241-9. (ICC; Human) [PubMed:23224884]

PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, Sato S, Hattori N. Scientific reports. 2012 2:1002. (WB; Mouse) [PubMed:23256036] [PMC:PMC3525937]

Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with Parkinson disease in mammalian cells and Drosophila. Song S, Jang S, Park J, Bang S, Choi S, Kwon KY, Zhuang X, Kim E, Chung J. The Journal of biological chemistry. 2013 288:5660-72. (ICC, WB; Human) [PubMed:23303188] [PMC:PMC3581423]

Mitochondrial Reprogramming Regulates Breast Cancer Progression. Kannan A, Wells RB, Sivakumar S, Komatsu S, Singh KP, Samten B, Philley JV, Sauter ER, Ikebe M, Idell S, Gupta S, Dasgupta S. Clinical cancer research : an official journal of the American Association for Cancer Research. 2016 22:3348-60. (WB; Human) [Full Text Article] [PubMed:26888829]

Complex-I Alteration and Enhanced Mitochondrial Fusion Are Associated With Prostate Cancer Progression. Philley JV, Kannan A, Qin W, Sauter ER, Ikebe M, Hertweck KL, Troyer DA, Semmes OJ, Dasgupta S. Journal of cellular physiology. 2016 June;231:1364-74. [Full Text Article] [PubMed:26530043] [PMC:PMC5741292]

Critical role of mitochondrial ubiquitination and the OPTN-ATG9A axis in mitophagy. Koji Yamano, Reika Kikuchi, Waka Kojima, Ryota Hayashida, Fumika Koyano, Junko Kawawaki, Takuji Shoda, Yosuke Demizu, Mikihiko Naito, Keiji Tanaka, Noriyuki Matsuda. The Journal of cell biology. 2020 September;219: [Full Text Article] [PubMed:32556086] [PMC:PMC7480101] Related Antibodies: LS-C96472.

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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).

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