Abstract
Chaperone-mediated autophagy (CMA) is a selective mechanism for degradation of soluble cytosolic proteins is responsible for the timed degradation of 30% of cytosolic proteins under conditions of prolonged nutrient deprivation and stress. Molecular chaperones in the lysosomal lumen and in the cytosol and induce this proteolytic pathway. A central molecule for CMA is a receptor in the lysosomal membrane is known as the lysosome-associated membrane protein (LAMP) type 2A. The decrease in CMA leads to cells to be more prone to oxidative stresses and pathogenes. Furthermore, the decreased CMA in aging is stem from reduced LAMP-2A in the lysosomal membrane. Here, we describe the evidence in support of the contribution of chaperokines and CMA in viral infections.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- CHIP:
-
Hsc70-interacting protein
- CMA:
-
Chaperone-mediated autophagy
- HCV:
-
Hepatitis C virus
- HSP:
-
Heat shock proteins
- IFNLR1:
-
Interferon α receptor 1
- LAMP-2A:
-
Lysosome-Associated Membrane Protein type 2A
- PERK:
-
PKR-like ER kinase
- UPR:
-
Unfolded protein response
- VSV:
-
Vesicular stomatitis virus
References
Agarraberes FA, Dice JF (2001) A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 114(13):2491–2499
Agarraberes FA, Terlecky SR, Dice JF (1997) An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 137(4):825–834
Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 28(18):5747–5763
Boya P, Reggiori F, Codogno P (2013) Emerging regulation and functions of autophagy. Nat Cell Biol 15(7):713
Brehme M, Voisine C (2016) Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity. Dis Model Mech 9(8):823–838
Chandra PK, Bao L, Song K, Aboulnasr FM, Baker DP, Shores N, Wimley WC, Liu S, Hagedorn CH, Fuchs SY (2014) HCV infection selectively impairs type I but not type III IFN signaling. Am J Pathol 184(1):214–229
Chiang H, Dice JF (1988) Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J Biol Chem 263(14):6797–6805
Chiang H-L, Terlecky SR, Plant CP, Dice JF (1989) A role for a 70-kilodaton heat shock protein in lysosomal degradation of intracellular proteins. Science 246(4928):382
Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10(2):86–103
Clough SJ, Bent AF (1998) Floral dip: a simplified method forAgrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16(6):735–743
Cohen-Kaplan V, Livneh I, Avni N, Cohen-Rosenzweig C, Ciechanover A (2016) The ubiquitin-proteasome system and autophagy: coordinated and independent activities. Int J Biochem Cell Biol 79:403–418
Crotzer VL, Glosson N, Zhou D, Nishino I, Blum JS (2010) LAMP-2-deficient human B cells exhibit altered MHC class II presentation of exogenous antigens. Immunology 131(3):318–330
Cuervo AM (2010) Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol Metab 21(3):142–150
Cuervo AM, Dice JF (1996) A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273(5274):501
Cuervo A, Knecht E, Terlecky SR, Dice JF (1995) Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Phys Cell Phys 269(5):C1200–C1208
Dash S, Chava S, Aydin Y, Chandra PK, Ferraris P, Chen W, Balart LA, Wu T, Garry RF (2016) Hepatitis C virus infection induces autophagy as a prosurvival mechanism to alleviate hepatic ER-stress response. Viruses 8(5):150
de Duve C (1963) Ciba foundation symposium on lysosomes (de Reuck AVS, Cameron MP, eds). JA Churchill Ltd., London
Dice JF (2007) Chaperone-mediated autophagy. Autophagy 3(4):295–299
Dice J, Chiang H, Spencer E, Backer J (1986) Regulation of catabolism of microinjected ribonuclease A. Identification of residues 7–11 as the essential pentapeptide. J Biol Chem 261(15):6853–6859
Feizi N, Mehrbod P, Romani B, Soleimanjahi H, Bamdad T, Feizi A, Jazaeri EO, Targhi HS, Saleh M, Jamali A (2017) Autophagy induction regulates influenza virus replication in a time-dependent manner. J Med Microbiol 66(4):536–541
Finn PF, Dice JF (2005) Ketone bodies stimulate chaperone-mediated autophagy. J Biol Chem 280(27):25864–25870
Gough NR, Hatem CL, Fambrough DM (1995) The family of LAMP-2 proteins arises by alternative splicing from a single gene: characterization of the avian LAMP-2 gene and identification of mammalian homologs of LAMP-2b and LAMP-2c. DNA Cell Biol 14(10):863–867
Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381(6583):571
Kettern N, Rogon C, Limmer A, Schild H, Höhfeld J (2011) The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells. PLoS One 6(1):e16398
Khateri M, Abdoli A, Motevalli F, Fotouhi F, Bolhassani A, Arashkia A, Jazaeri EO, Shahbazi S, Mehrbod P, Naziri H (2018) Evaluation of autophagy induction on HEV 239 vaccine immune response in a mouse model. IUBMB Life 70:207–214
Kurt R, Chandra PK, Aboulnasr F, Panigrahi R, Ferraris P, Aydin Y, Reiss K, Wu T, Balart LA, Dash S (2015) Chaperone-mediated autophagy targets IFNAR1 for lysosomal degradation in free fatty acid treated HCV cell culture. PLoS One 10(5):e0125962
Liu J, HuangFu W-C, Kumar KS, Qian J, Casey JP, Hamanaka RB, Grigoriadou C, Aldabe R, Diehl JA, Fuchs SY (2009) Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor. Cell Host Microbe 5(1):72–83
Malhotra JD, Kaufman RJ (2007) The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 18:716–731
Salvador N, Aguado C, Horst M, Knecht E (2000) Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 275(35):27447–27456
Slavotinek AM, Biesecker LG (2001) Unfolding the role of chaperones and chaperonins in human disease. Trends Genet 17(9):528–535
Taji F, Kouchesfahani HM, Sheikholeslami F, Romani B, Baesi K, Vahabpour R, Edalati M, Teimoori-Toolabi L, Jazaeri EO, Abdoli A (2017) Autophagy induction reduces telomerase activity in HeLa cells. Mech Ageing Dev 163:40–45
Wang D-w, Peng Z-j, Ren G-f, Wang G-x (2015) The different roles of selective autophagic protein degradation in mammalian cells. Oncotarget 6(35):37098
Waris G, Tardif KD, Siddiqui A (2002) Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-κB and STAT-3. Biochem Pharmacol 64(10):1425–1430
Welihinda AA, Tirasophon W, Kaufman RJ (1999) The cellular response to protein misfolding in the endoplasmic reticulum. Gene Expr 7(4–5):293–300
Willis MS, Patterson C (2010) Hold me tight: role of the heat shock protein family of chaperones in cardiac disease. Circulation 122(17):1740–1751
Wondrak GT (2015) Stress response pathways in cancer. Springer, Netherlands
Yan MM, Ni JD, Song D, Ding M, Huang J (2015) Interplay between unfolded protein response and autophagy promotes tumor drug resistance. Oncol Lett 10(4):1959–1969
Zhou D, Li P, Lin Y, Lott JM, Hislop AD, Canaday DH, Brutkiewicz RR, Blum JS (2005) Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 22(5):571–581
Acknowledgments
We would like to thank all members of virology department of Tarbiat Modares University and Hepatitis and AIDS department of Pasteur Institute for kind assistant and support.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Soleimanjahi, H., Abdoli, A. (2019). Role of Chaperone Mediated Autophagy in Viral Infections. In: Asea, A., Kaur, P. (eds) Chaperokine Activity of Heat Shock Proteins . Heat Shock Proteins, vol 16. Springer, Cham. https://doi.org/10.1007/978-3-030-02254-9_7
Download citation
DOI: https://doi.org/10.1007/978-3-030-02254-9_7
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-02253-2
Online ISBN: 978-3-030-02254-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)