LETTER

Ubiquitin is double-phosphorylated by PINK1 for enhanced pH-sensitivity of conformational switch

  • Shang-Xiang Ye 1 ,
  • Zhou Gong 2 ,
  • Ju Yang 2 ,
  • Yu-Xin An 4 ,
  • Zhu Liu 2 ,
  • Qun Zhao 4 ,
  • Ewen Lescop 3 ,
  • Xu Dong , 2 ,
  • Chun Tang , 1,2
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  • 1. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China
  • 2. CAS Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Resonance at Wuhan, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, Wuhan 430071, China
  • 3. Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Univ Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France
  • 4. CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics of the Chinese Academy of Sciences, Dalian 116023, China

Published date: 15 Dec 2019

Copyright

2019 The Author(s)

Cite this article

Shang-Xiang Ye , Zhou Gong , Ju Yang , Yu-Xin An , Zhu Liu , Qun Zhao , Ewen Lescop , Xu Dong , Chun Tang . Ubiquitin is double-phosphorylated by PINK1 for enhanced pH-sensitivity of conformational switch[J]. Protein & Cell, 2019 , 10(12) : 908 -913 . DOI: 10.1007/s13238-019-0644-x

1
Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD (2015) Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. Nature 519:106–109

DOI

2
Berezhnov AV, Soutar MP, Fedotova EI, Frolova MS, Plun-Favreau H, Zinchenko VP, Abramov AY (2016) Intracellular pH modulates autophagy and mitophagy. J Biol Chem 291:8701–8708

DOI

3
Bienkiewicz EA, Lumb KJ (1999) Random-coil chemical shifts of phosphorylated amino acids. J Biomol NMR 15:203–206

DOI

4
Dong X, Gong Z, Lu Y-B, Liu K, Qin L-Y, Ran M-L, Zhang C-L, Liu Z, Zhang W-P, Tang C (2017) Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch. Proc Natl Acad Sci USA 114:6770–6775

DOI

5
Gao J, Li M, Qin S, Zhang T, Jiang S, Hu Y, Deng Y, Zhang C, You D, Li H (2016) Cytosolic PINK1 promotes the targeting of ubiquitinated proteins to the aggresome-autophagy pathway during proteasomal stress. Autophagy 12:632–647

DOI

6
Gladkova C, Schubert AF, Wagstaff JL, Pruneda JN, Freund SM, Komander D (2017) An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1. EMBO J 36:3555–3572

DOI

7
Gladkova C, Maslen SL, Skehel JM, Komander D (2018) Mechanism of parkin activation by PINK1. Nature 559:410–414

DOI

8
Kane LA, Lazarou M, Fogel AI, Li Y, Yamano K, Sarraf SA, Banerjee S, Youle RJ (2014) PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol 205:143–153

DOI

9
Kapuy O, Barik D, Sananes MR, Tyson JJ, Novak B (2009) Bistability by multiple phosphorylation of regulatory proteins. Prog Biophys Mol Biol 100:47–56

DOI

10
Koyano F, Okatsu K, Kosako H, Tamura Y, Go E, Kimura M, Kimura Y, Tsuchiya H, Yoshihara H, Hirokawa T (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510:162–166

DOI

11
Liu Z, Gong Z, Dong X, Tang C (2016) Transient protein-protein interactions visualized by solution NMR. Biochim Biophys Acta Proteins Proteomics 1864:115–122

DOI

12
Okatsu K, Sato Y, Yamano K, Matsuda N, Negishi L, Takahashi A, Yamagata A, Goto-Ito S, Mishima M, Ito Y (2018) Structural insights into ubiquitin phosphorylation by PINK1. Sci Rep 8:10382

DOI

13
Schoppa NE, McCormack K, Tanouye MA, Sigworth FJ (1992) The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255:1712–1715

DOI

14
Swatek KN, Komander D (2016) Ubiquitin modifications. Cell Res 26:399–422

DOI

15
White KA, Grillo-Hill BK, Barber DL (2017) Cancer cell behaviors mediated by dysregulated pH dynamics at a glance. J Cell Sci 130:663–669

DOI

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