The Role of K63-linked Polyubiquitin in Several Types of Autophagy

Overview

Journal Biol Futur

Specialty Biology

Date 2022 May 2

PMID 35501575

Authors

Anna Dosa

Tamas Csizmadia

Affiliations

Soon will be listed here.

Abstract

Lysosomal-dependent self-degradative (autophagic) mechanisms are essential for the maintenance of normal homeostasis in all eukaryotic cells. Several types of such self-degradative and recycling pathways have been identified, based on how the cellular self material can incorporate into the lysosomal lumen. Ubiquitination, a well-known and frequently occurred posttranslational modification has essential role in all cell biological processes, thus in autophagy too. The second most common type of polyubiquitin chain is the K63-linked polyubiquitin, which strongly connects to some self-degradative mechanisms in the cells. In this review, we discuss the role of this type of polyubiquitin pattern in numerous autophagic processes.

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References

Ahlberg J, Beije B, Berkenstam A, Henell F, Glaumann H . Effects on in vivo and in vitro administration of vinblastine on the perfused rat liver--identification of crinosomes. Exp Mol Pathol. 1987; 47(3):309-26. DOI: 10.1016/0014-4800(87)90016-5. View

Badarudeen B, Anand U, Mukhopadhyay S, Manna T . Ubiquitin signaling in the control of centriole duplication. FEBS J. 2021; 289(16):4830-4849. DOI: 10.1111/febs.16069. View

Bhattacharjee A, Szabo A, Csizmadia T, Laczko-Dobos H, Juhasz G . Understanding the importance of autophagy in human diseases using Drosophila. J Genet Genomics. 2019; 46(4):157-169. DOI: 10.1016/j.jgg.2019.03.007. View

Bhattacharyya S, Yu H, Mim C, Matouschek A . Regulated protein turnover: snapshots of the proteasome in action. Nat Rev Mol Cell Biol. 2014; 15(2):122-33. PMC: 4384331. DOI: 10.1038/nrm3741. View

Chen Z, Sun L . Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell. 2009; 33(3):275-86. DOI: 10.1016/j.molcel.2009.01.014. View

Clague M, Urbe S . Integration of cellular ubiquitin and membrane traffic systems: focus on deubiquitylases. FEBS J. 2017; 284(12):1753-1766. PMC: 5484354. DOI: 10.1111/febs.14007. View

Clague M, Barsukov I, Coulson J, Liu H, Rigden D, Urbe S . Deubiquitylases from genes to organism. Physiol Rev. 2013; 93(3):1289-315. DOI: 10.1152/physrev.00002.2013. View

Clague M, Heride C, Urbe S . The demographics of the ubiquitin system. Trends Cell Biol. 2015; 25(7):417-26. DOI: 10.1016/j.tcb.2015.03.002. View

Clough B, Wright J, Pereira P, Hirst E, Johnston A, Henriques R . K63-Linked Ubiquitination Targets Toxoplasma gondii for Endo-lysosomal Destruction in IFNγ-Stimulated Human Cells. PLoS Pathog. 2016; 12(11):e1006027. PMC: 5119857. DOI: 10.1371/journal.ppat.1006027. View

10.

Coux O, Zieba B, Meiners S . The Proteasome System in Health and Disease. Adv Exp Med Biol. 2020; 1233:55-100. DOI: 10.1007/978-3-030-38266-7_3. View

11.

Csizmadia T, Juhasz G . Crinophagy mechanisms and its potential role in human health and disease. Prog Mol Biol Transl Sci. 2020; 172:239-255. DOI: 10.1016/bs.pmbts.2020.02.002. View

12.

Csizmadia T, Lorincz P, Hegedus K, Szeplaki S, Low P, Juhasz G . Molecular mechanisms of developmentally programmed crinophagy in . J Cell Biol. 2017; 217(1):361-374. PMC: 5748974. DOI: 10.1083/jcb.201702145. View

13.

Cuervo A, Wong E . Chaperone-mediated autophagy: roles in disease and aging. Cell Res. 2013; 24(1):92-104. PMC: 3879702. DOI: 10.1038/cr.2013.153. View

14.

Deng L, Wang C, Spencer E, Yang L, Braun A, You J . Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell. 2000; 103(2):351-61. DOI: 10.1016/s0092-8674(00)00126-4. View

15.

Denton D, Kumar S . Autophagy-dependent cell death. Cell Death Differ. 2018; 26(4):605-616. PMC: 6460387. DOI: 10.1038/s41418-018-0252-y. View

16.

Dickey C, Kamal A, Lundgren K, Klosak N, Bailey R, Dunmore J . The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest. 2007; 117(3):648-58. PMC: 1794119. DOI: 10.1172/JCI29715. View

17.

Dikic I . Proteasomal and Autophagic Degradation Systems. Annu Rev Biochem. 2017; 86:193-224. DOI: 10.1146/annurev-biochem-061516-044908. View

18.

Emmerich C, Ordureau A, Strickson S, Arthur J, Pedrioli P, Komander D . Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains. Proc Natl Acad Sci U S A. 2013; 110(38):15247-52. PMC: 3780889. DOI: 10.1073/pnas.1314715110. View

19.

Erpapazoglou Z, Walker O, Haguenauer-Tsapis R . Versatile roles of k63-linked ubiquitin chains in trafficking. Cells. 2014; 3(4):1027-88. PMC: 4276913. DOI: 10.3390/cells3041027. View

20.

Figueira R, Brown D, Ferreira D, Eldridge M, Burchell L, Pan Z . Adaptation to sustained nitrogen starvation by Escherichia coli requires the eukaryote-like serine/threonine kinase YeaG. Sci Rep. 2015; 5:17524. PMC: 4664914. DOI: 10.1038/srep17524. View