Abstract
Autophagy is a lysosome-dependent degradation process. During autophagy, cytoplasmic components are sequestered and catabolized to supply nutrition and energy under starvation conditions. Recent work has demonstrated that many cargos can be specifically recognized and then eliminated via the core mechanism of autophagy which is termed as selective autophagy. The cargo recognition program provides the basis for the specific degradation of selective autophagy; thus, the exploration of the interaction between the cargo and the receptor is the key for revealing the underlying mechanism. Also, receptor protein complexes are required in various selective autophagy subtypes which process and guide the cargo to the core mechanism. Ubiquitination and phosphorylation are the main methods to modulate the affinity of the receptor toward cargo. Although many key processes of selective autophagy subtypes have been discovered and intensively studied, the precise ways in which the mechanisms of cargo recognition function remain mostly elusive. A fuller mechanistic understanding of selective autophagy will be important for efforts to promote disease treatment and drug development.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Akinduro O, Sully K, Patel A, Robinson DJ, Chikh A, McPhail G, Braun KM, Philpott MP, Harwood CA, Byrne C, O’shaughnessy RFL, Bergamaschi D. Constitutive autophagy and nucleophagy during epidermal differentiation. J Invest Dermatol. 2016;136:1460–70.
Birgisdottir AB, Lamark T, Johansen T. The Lir motif—crucial for selective autophagy. J Cell Sci. 2013;126:3237–47.
Deng Z, Purtell K, Lachance V, Wold MS, Chen S, Yue Z. Autophagy receptors and neurodegenerative diseases. Trends Cell Biol. 2017;27:491–504.
Fu T, Liu J, Wang Y, Xie X, Hu S, Pan L. Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1. Proc Natl Acad Sci U S A. 2018;115:E11651–60.
Gladkova C, Maslen SL, Skehel JM, Komander D. Mechanism of parkin activation by PINK1. Nature. 2018;559:410–4.
Kaushik S, Cuervo AM. The coming of age of chaperone-mediated autophagy. Nat Rev Mol Cell Biol. 2018;19:365–81.
Khaminets A, Behl C, Dikic I. Ubiquitin-dependent and independent signals in selective autophagy. Trends Cell Biol. 2016;26:6–16.
Kraft C, Deplazes A, Sohrmann M, Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol. 2008;10:602–10.
Lahiri V, Klionsky DJ. CCPG1 is a noncanonical autophagy cargo receptor essential for reticulophagy and pancreatic ER proteostasis. Autophagy. 2018;14(7):1107–1109.
Liu L, Feng D, Chen G, Chen M, Zheng Q, Song P, Ma Q, Zhu C, Wang R, Qi W, Huang L, Xue P, Li B, Wang X, Jin H, Wang J, Yang F, Liu P, Zhu Y, Sui S, Chen Q. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat Cell Biol. 2012;14:177–85.
Liu L, Sakakibara K, Chen Q, Okamoto K. Receptor-mediated mitophagy in yeast and mammalian systems. Cell Res. 2014;24:787–95.
Lv L, Li D, Zhao D, Lin R, Chu Y, Zhang H, Zha Z, Liu Y, Li Z, Xu Y, Wang G, Huang Y, Xiong Y, Guan KL, Lei QY. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol Cell. 2011;42:719–30.
Lynch-Day MA, Klionsky DJ. The Cvt pathway as a model for selective autophagy. FEBS Lett. 2010;584:1359–66.
Maejima I, Takahashi A, Omori H, Kimura T, Takabatake Y, Saitoh T, Yamamoto A, Hamasaki M, Noda T, Isaka Y, Yoshimori T. Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury. EMBO J. 2013;32:2336–47.
Mancias JD, Wang X, Gygi SP, Harper JW, Kimmelman AC. Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy. Nature. 2014;509:105–9.
Mancias JD, Pontano Vaites L, Nissim S, Biancur DE, Kim AJ, Wang X, Liu Y, Goessling W, Kimmelman AC, Harper JW. Ferritinophagy via Ncoa4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis. Elife. 2015;4:e10308.
Mochida K, Oikawa Y, Kimura Y, Kirisako H, Hirano H, Ohsumi Y, Nakatogawa H. Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus. Nature. 2015;522:359–62.
Nakatogawa H, Mochida K. Reticulophagy and nucleophagy: new findings and unsolved issues. Autophagy. 2015;11:2377–8.
Noda T, Kageyama S, Fujita N, Yoshimori T. Three-Axis model for Atg recruitment in autophagy against Salmonella. Int J Cell Biol. 2012;2012:389562.
Santana-Codina N, Mancias JD. The role of NCOA4-mediated ferritinophagy in health and disease. Pharmaceuticals (Basel). 2018;11:114.
Singh R, Kaushik S, Wang Y, Xiang Y, Novak I, Komatsu M, Tanaka K, Cuervo AM, Czaja MJ. Autophagy regulates lipid metabolism. Nature. 2009;458:1131–5.
Stolz A, Ernst A, Dikic I. Cargo recognition and trafficking in selective autophagy. Nat Cell Biol. 2014;16:495–501.
Sturner E, Behl C. The role of the multifunctional BAG3 protein in cellular protein quality control and in disease. Front Mol Neurosci. 2017;10:177.
Tan S, Wong E. Kinetics of protein aggregates disposal by aggrephagy. Methods Enzymol. 2017;588:245–81.
Wyant GA, Abu-Remaileh M, Frenkel EM, Laqtom NN, Dharamdasani V, Lewis CA, Chan SH, Heinze I, Ori A, Sabatini DM. NUFIP1 is a ribosome receptor for starvation-induced ribophagy. Science. 2018;360:751–8.
Yamasaki A, Noda NN. Structural biology of the Cvt pathway. J Mol Biol. 2017;429:531–42.
Zhang J, Tripathi DN, Jing J, Alexander A, Kim J, Powell RT, Dere R, Tait-Mulder J, Lee JH, Paull TT, Pandita RK, Charaka VK, Pandita TK, Kastan MB, Walker CL. ATM functions at the peroxisome to induce pexophagy in response to ROS. Nat Cell Biol. 2015;17:1259–69.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2021 Science Press
About this chapter
Cite this chapter
Fan, QW., Yan, XH. (2021). Mechanisms of Selective Autophagy. In: Xie, Z. (eds) Autophagy: Biology and Diseases. Advances in Experimental Medicine and Biology, vol 1208. Springer, Singapore. https://doi.org/10.1007/978-981-16-2830-6_6
Download citation
DOI: https://doi.org/10.1007/978-981-16-2830-6_6
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-16-2829-0
Online ISBN: 978-981-16-2830-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)