Histone deacetylase 10 knockout activates chaperone-mediated autophagy and accelerates the decomposition of its substrate

[1] B. Levine, G. Kroemer, Autophagy in the pathogenesis of disease, Cell 132

(2008) 27e42, https://doi.org/10.1016/j.cell.2007.12.018.

[2] N. Mizushima, B. Levine, A.M. Cuervo, D.J. Klionsky, Autophagy fights disease

through cellular self-digestion, Nature 451 (2008) 1069e1075, https://doi.org/

10.1038/nature06639.

[3] N. Mizushima, B. Levine, Autophagy in mammalian development and differentiation, Nat. Cell Biol. 12 (2010) 823e830, https://doi.org/10.1038/ncb0910823.

[4] N. Mizushima, M. Komatsu, Autophagy: renovation of cells and tissues, Cell

147 (2011) 728e741, https://doi.org/10.1016/j.cell.2011.10.026.

[5] J.B. Kunz, H. Schwarz, A. Mayer, Determination of four sequential stages

during microautophagy in vitro, J. Biol. Chem. 279 (2004) 9987e9996, https://

doi.org/10.1074/jbc.M307905200.

[6] S.J. Orenstein, A.M. Cuervo, Chaperone-mediated autophagy: molecular

mechanisms and physiological relevance, Semin. Cell Dev. Biol. 21 (2010)

719e726, https://doi.org/10.1016/j.semcdb.2010.02.005.

[7] S. Kaushik, A.M. Cuervo, The coming of age of chaperone-mediated autophagy,

Nat. Rev. Mol. Cell Biol. 19 (2018) 365e381, https://doi.org/10.1038/s41580018-0001-6.

[8] G. Pinto, B. Shtaif, M. Phillip, G. Gat-Yablonski, Growth attenuation is associated with histone deacetylase 10-induced autophagy in the liver, J. Nutr.

Biochem. 27 (2016) 171e180, https://doi.org/10.1016/j.jnutbio.2015.08.031.

[9] A.R. Guardiola, T.P. Yao, Molecular cloning and characterization of a novel

histone deacetylase HDAC10, J. Biol. Chem. 277 (2002) 3350e3356, https://

doi.org/10.1074/jbc.M109861200.

[10] S. Kotian, S. Liyanarachchi, A. Zelent, J.D. Parvin, Histone deacetylases 9 and 10

are required for homologous recombination, J. Biol. Chem. 286 (2011)

7722e7726, https://doi.org/10.1074/jbc.C110.194233.

[11] C. Song, S. Zhu, C. Wu, J. Kang, Histone deacetylase (HDAC) 10 suppresses

cervical cancer metastasis through inhibition of matrix metalloproteinase

(MMP) 2 and 9 expression, J. Biol. Chem. 288 (2013) 28021e28033, https://

doi.org/10.1074/jbc.M113.498758.

[12] Y. Li, L. Peng, E. Seto, Histone deacetylase 10 regulates the cell cycle G2/M

phase transition via a novel Let-7-HMGA2-Cyclin A2 pathway, Mol. Cell. Biol.

35 (2015) 3547e3565, https://doi.org/10.1128/mcb.00400-15.

[13] I. Oehme, J.P. Linke, B.C. Bock, T. Milde, M. Lodrini, B. Hartenstein, I. Wiegand,

C. Eckert, W. Roth, M. Kool, S. Kaden, H.J. Grone, J.H. Schulte, S. Lindner,

A. Hamacher-Brady, N.R. Brady, H.E. Deubzer, O. Witt, Histone deacetylase 10

promotes autophagy-mediated cell survival, Proc. Natl. Acad. Sci. U.S.A. 110

(2013) E2592eE2601, https://doi.org/10.1073/pnas.1300113110.

[14] I.L. Lai, T.P. Lin, Y.L. Yao, C.Y. Lin, M.J. Hsieh, W.M. Yang, Histone deacetylase 10

relieves repression on the melanogenic program by maintaining the deacetylation status of repressors, J. Biol. Chem. 285 (2010) 7187e7196, https://

doi.org/10.1074/jbc.M109.061861.

[15] T. Seki, K.I. Yoshino, S. Tanaka, E. Dohi, T. Onji, K. Yamamoto, I. Hide,

H.L. Paulson, N. Saito, N. Sakai, Establishment of a novel fluorescence-based

method to evaluate chaperone-mediated autophagy in a single neuron,

PLoS One 7 (2012), e31232, https://doi.org/10.1371/journal.pone.0031232.

[16] E. Arias, Methods to study chaperone-mediated autophagy, Methods Enzymol. 588 (2017) 283e305, https://doi.org/10.1016/bs.mie.2016.10.009.

[17] S. Kaushik, A.M. Cuervo, Methods to monitor chaperone-mediated autophagy,

Methods Enzymol. 452 (2009) 297e324, https://doi.org/10.1016/s00766879(08)03619-7.

[18] E. Dohi, S. Tanaka, T. Seki, T. Miyagi, I. Hide, T. Takahashi, M. Matsumoto,

N. Sakai, Hypoxic stress activates chaperone-mediated autophagy and modulates neuronal cell survival, Neurochem. Int. 60 (2012) 431e442, https://

doi.org/10.1016/j.neuint.2012.01.020.

[19] P. Jiang, N. Mizushima, LC3- and p62-based biochemical methods for the

analysis of autophagy progression in mammalian cells, Methods 75 (2015)

13e18, https://doi.org/10.1016/j.ymeth.2014.11.021.

[20] F. Stricher, C. Macri, M. Ruff, S. Muller, HSPA8/HSC70 chaperone protein:

structure, function, and chemical targeting, Autophagy 9 (2013) 1937e1954,

https://doi.org/10.4161/auto.26448.

[21] F.A. Agarraberes, S.R. Terlecky, J.F. Dice, An intralysosomal hsp 70 is required

for a selective pathway of lysosomal protein degradation, J. Cell Biol. 137

(1997) 825e834, https://doi.org/10.1083/jcb.137.4.825.

Please cite this article as: H. Obayashi et al., Histone deacetylase 10 knockout activates chaperone-mediated autophagy and accelerates the

decomposition of its substrate, Biochemical and Biophysical Research Communications, https://doi.org/10.1016/j.bbrc.2019.12.048

H. Obayashi et al. / Biochemical and Biophysical Research Communications xxx (xxxx) xxx

[22] N. Salvador, C. Aguado, M. Horst, E. Knecht, Import of a cytosolic protein into

lysosomes by chaperone-mediated autophagy depends on its folding state,

J. Biol. Chem. 275 (2000) 27447e27456, https://doi.org/10.1074/

jbc.M001394200.

[23] F.A. Agarraberes, J.F. Dice, A molecular chaperone complex at the lysosomal

membrane is required for protein translocation, J. Cell Sci. 114 (2001)

2491e2499.

[24] A.M. Cuervo, J.F. Dice, E. Knecht, A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins, J. Biol.

Chem. 272 (1997) 5606e5615, https://doi.org/10.1074/jbc.272.9.5606.

[25] U. Bandyopadhyay, S. Sridhar, S. Kaushik, R. Kiffin, A.M. Cuervo, Identification

of regulators of chaperone-mediated autophagy, Mol. Cell 39 (2010) 535e547,

https://doi.org/10.1016/j.molcel.2010.08.004.

[26] E. Arias, H. Koga, A. Diaz, E. Mocholi, B. Patel, A.M. Cuervo, Lysosomal

mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy, Mol. Cell 59

(2015) 270e284, https://doi.org/10.1016/j.molcel.2015.05.030.

[27] Y. Yang, Y. Huang, Z. Wang, H.T. Wang, B. Duan, D. Ye, C. Wang, R. Jing, Y. Leng,

J. Xi, W. Chen, G. Wang, W. Jia, S. Zhu, J. Kang, HDAC10 promotes lung cancer

proliferation via AKT phosphorylation, Oncotarget 7 (2016) 59388e59401,

https://doi.org/10.18632/oncotarget.10673.

[28] S. Saito, Y. Zhuang, B. Shan, S. Danchuk, F. Luo, M. Korfei, A. Guenther,

J.A. Lasky, Tubastatin ameliorates pulmonary fibrosis by targeting the

TGFbeta-PI3K-Akt pathway, PLoS One 12 (2017), e0186615, https://doi.org/

10.1371/journal.pone.0186615.

[29] R. Sahu, S. Kaushik, C.C. Clement, E.S. Cannizzo, B. Scharf, A. Follenzi,

I. Potolicchio, E. Nieves, A.M. Cuervo, L. Santambrogio, Microautophagy of

cytosolic proteins by late endosomes, Dev. Cell 20 (2011) 131e139, https://

doi.org/10.1016/j.devcel.2010.12.003.

[30] M. Sato, T. Seki, A. Konno, H. Hirai, Y. Kurauchi, A. Hisatsune, H. Katsuki,

Fluorescent-based evaluation of chaperone-mediated autophagy and microautophagy activities in cultured cells, Genes Cells 21 (2016) 861e873, https://

doi.org/10.1111/gtc.12390.

Please cite this article as: H. Obayashi et al., Histone deacetylase 10 knockout activates chaperone-mediated autophagy and accelerates the

decomposition of its substrate, Biochemical and Biophysical Research Communications, https://doi.org/10.1016/j.bbrc.2019.12.048

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