References
- Martini-Stoica H, Xu Y, Ballabio A, et al. The Autophagy-lysosomal pathway in neurodegeneration: a TFEB perspective. Trends Neurosci. 2016;39:221–234.
- Tsunemi T, Ashe TD, Morrison BE, et al. PGC-1alpha rescues Huntington’s disease proteotoxicity by preventing oxidative stress and promoting TFEB function. Sci Transl Med. 2012;4:142ra97.
- Thompson LM, Aiken CT, Kaltenbach LS, et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J Cell Biol. 2009;187:1083–1099.
- Rui YN, Xu Z, Patel B, et al. Huntingtin functions as a scaffold for selective macroautophagy. Nat Cell Biol. 2015;17:262–275.
- Ross CA, Tabrizi SJ. Huntington’s disease: from molecular pathogenesis to clinical treatment. Lancet Neurol. 2011;10:83–98.
- Qi L, Zhang XD, Wu JC, et al. The role of chaperone-mediated autophagy in huntingtin degradation. PLoS One. 2012;7:e46834.
- Ochaba J, Lukacsovich T, Csikos G, et al. Potential function for the Huntingtin protein as a scaffold for selective autophagy. Proc Natl Acad Sci USA. 2014;111:16889–16894.
- Martinez-Vicente M, Talloczy Z, Wong E, et al. Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease. Nat Neurosci. 2010;13:567–576.
- Menzies FM, Fleming A, Rubinsztein DC. Compromised autophagy and neurodegenerative diseases. Nat Rev Neurosci. 2015;16:345–357.
- Gozuacik D, Akkoc Y, Ozturk DG, et al. Autophagy-regulating microRNAs and cancer. Front Oncol. 2017;7:65.
- Napolitano G, Ballabio A. TFEB at a glance. J Cell Sci. 2016;129:2475–2481.
- Rehli M, Den Elzen N, Cassady AI, et al. Cloning and characterization of the murine genes for bHLH-ZIP transcription factors TFEC and TFEB reveal a common gene organization for all MiT subfamily members. Genomics. 1999;56:111–120.
- Settembre C, Di MC, Va P, et al. TFEB links autophagy to lysosomal biogenesis. Science. 2011;332:1429–1433.
- Roczniak-Ferguson A, Petit CS, Froehlich F, et al. The transcription factor TFEB links MTORC1 signaling to transcriptional control of lysosome homeostasis. Sci Signal. 2012;5:ra42.
- Palmieri M, Impey S, Kang H, et al. Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum Mol Genet. 2011;20:3852–3866.
- Pena-Llopis S, Vega-Rubin-de-Celis S, Schwartz JC, et al. Regulation of TFEB and V-ATPases by MTORC1. Embo J. 2011;30:3242–3258.
- Martina JA, Chen Y, Gucek M, et al. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy. 2012;8:903–914.
- Medina DL, Di Paola S, Peluso I, et al. Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB. Nat Cell Biol. 2015;17:288–299.
- Wilker EW, Grant RA, Artim SC, et al. A structural basis for 14-3-3sigma functional specificity. J Biol Chem. 2005;280:18891–18898.
- Tzivion G, Avruch J. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem. 2002;277:3061–3064.
- Tong Y, Song F. Intracellular calcium signaling regulates autophagy via calcineurin-mediated TFEB dephosphorylation. Autophagy. 2015;11:1192–1195.
- Rittinger K, Budman J, Xu J, et al. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell. 1999;4:153–166.
- Muslin AJ, Tanner JW, Allen PM, et al. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell. 1996;84:889–897.
- Yaffe MB, Rittinger K, Volinia S, et al. The structural basis for 14-3-3: phosphopeptidebinding specificity. Cell. 1997;91:961–971.
- Ottmann C, Yasmin L, Weyand M, et al. Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Embo J. 2007;26:902–913.
- Choe JY, Nelson SW, Arienti KL, et al. Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors. J Biol Chem. 2003;278:51176–51183.
- Pogenberg V, Ogmundsdottir MH, Bergsteinsdottir K, et al. Restricted leucine zipper dimerization and specificity of DNA recognition of the melanocyte master regulator MITF. Genes Dev. 2012;26:2647–2658.
- Wang QS, Yu F, Huang S, et al. The macromolecular crystallography beamline of SSRF. Nucl Sci Tech. 2015;26:12–17.
- Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997;276:307–326.
- McCoy AJ. Solving structures of protein complexes by molecular replacement with phaser. Acta Crystallogr D Biol Crystallogr. 2007;63:32–41.
- Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr. 2004;60:2126–2132.
- Adams PD, Afonine PV, Bunkoczi G, et al. PHENIX: a comprehensive python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr. 2010;66:213–221.
- Laskowski RA, Macarthur MW, Moss DS, et al. Procheck - a program to check the stereochemical quality of protein structures. J Appl Crystallogr. 1993;26:283–291.
- Gietz RD, Schiestl RH. High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method. Nat Protoc. 2007;2:31–34.