Measuring Cysteine Exposure in Unfolded Proteins with Tetraphenylethene Maleimide and its Analogs.
Aggregation-induced emission
Cysteine exposure
Protein footprinting
Proteostasis
Unfolded protein
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
5
1
2022
pubmed:
6
1
2022
medline:
30
3
2022
Statut:
ppublish
Résumé
When proteostasis is challenged and becomes unbalanced, unfolded proteins can accumulate in the cells. Protein unfolding causes conformational changes and subsequent differentials in side-chain solvent accessibility and reactivity. In particular, when protein unfolds, non-disulfide-bonded cysteines that are usually buried in the native state can become surface exposed and thus accessible. A series of fluorogenic dyes including tetraphenylethene maleimide (TPE-MI) and its analogs were developed to capture cysteine exposure in unfolded proteins as a measure of unfolded protein load and proteostasis capacity in cells. These dyes are inherently non-fluorescent but show fluorescence turn-on effect when conjugated to unfolded proteins via reacting with exposed cysteines on the protein. Reacting with small biothiols such as glutathione does not induce fluorescence of these dyes. Here we describe the routine workflow to characterize unfolded proteins in vitro or unfolded proteomes in cells by TPE-MIs.
Identifiants
pubmed: 34985690
doi: 10.1007/978-1-0716-1732-8_1
doi:
Substances chimiques
Fluorescent Dyes
0
Maleimides
0
Proteome
0
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3-18Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Sebastian RM, Shoulders MD (2020) Chemical biology framework to illuminate proteostasis. Annu Rev Biochem 89:529–555
doi: 10.1146/annurev-biochem-013118-111552
pubmed: 32097570
pmcid: 7311290
Oakes SA, Papa FR (2015) The role of endoplasmic reticulum stress in human pathology. Annu Rev Pathol 10:173–194
doi: 10.1146/annurev-pathol-012513-104649
pubmed: 25387057
Karagöz GE, Acosta-Alvear D, Walter P (2019) The unfolded protein response: detecting and responding to fluctuations in the protein-folding capacity of the endoplasmic reticulum. Cold Spring Harb Perspect Biol 11(9):a033886
doi: 10.1101/cshperspect.a033886
pubmed: 30670466
pmcid: 6719602
Nam SM, Jeon YJ (2019) Proteostasis in the endoplasmic reticulum: road to cure. Cancers (Basel) 11
Balch WE, Morimoto RI, Dillin A, Kelly JW (2008) Adapting proteostasis for disease intervention. Science 319:916–919
doi: 10.1126/science.1141448
pubmed: 18276881
Klaips CL, Jayaraj GG, Hartl FU (2018) Pathways of cellular proteostasis in aging and disease. J Cell Biol 217:51–63
doi: 10.1083/jcb.201709072
pubmed: 29127110
pmcid: 5748993
Wang HW, Wang JW (2017) How cryo-electron microscopy and X-ray crystallography complement each other. Protein Sci 26:32–39
doi: 10.1002/pro.3022
pubmed: 27543495
Hipp MS, Kasturi P, Hartl FU (2019) The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20:421–435
doi: 10.1038/s41580-019-0101-y
pubmed: 30733602
Wang L, Chance MR (2017) Protein footprinting comes of age: mass spectrometry for biophysical structure assessment. Mol Cell Proteomics 16:706–716
doi: 10.1074/mcp.O116.064386
pubmed: 28275051
pmcid: 5417815
Kostyukevich Y, Acter T, Zherebker A, Ahmed A, Kim S, Nikolaev E (2018) Hydrogen/deuterium exchange in mass spectrometry. Mass Spectrom Rev 37:811–853
doi: 10.1002/mas.21565
pubmed: 29603316
Maleknia SD, Downard KM (2019) Protein footprinting with radical probe mass spectrometry- two decades of achievement. Protein Pept Lett 26:4–15
doi: 10.2174/0929866526666181128124241
pubmed: 30484400
Marino SM, Gladyshev VN (2010) Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces. J Mol Biol 404:902–916
doi: 10.1016/j.jmb.2010.09.027
pubmed: 20950627
pmcid: 3061813
Chen MZ, Moily NS, Bridgford JL, Wood RJ, Radwan M, Smith TA, Song Z, Tang BZ, Tilley L, Xu X, Reid GE, Pouladi MA, Hong Y, Hatters DM (2017) A thiol probe for measuring unfolded protein load and proteostasis in cells. Nat Commun 8:474
doi: 10.1038/s41467-017-00203-5
pubmed: 28883394
pmcid: 5589734
Francis MB, Carrico IS (2010) New frontiers in protein bioconjugation. Curr Opin Chem Biol 14:771–773
doi: 10.1016/j.cbpa.2010.11.006
pubmed: 21112236
Zhao Z, Lam JWY, Tang BZ (2012) Tetraphenylethene: a versatile AIE building block for the construction of efficient luminescent materials for organic light-emitting diodes. J Mater Chem 22:23726–23740
doi: 10.1039/c2jm31949g
Hong Y, Lam JWY, Tang BZ (2009) Aggregation-induced emission: phenomenon, mechanism and applications. Chem Commun 29:4332–4353
doi: 10.1039/b904665h
Hong Y, Lam JWY, Tang BZ (2011) Aggregation-induced emission. Chem Soc Rev 40:5361–5388
doi: 10.1039/c1cs15113d
pubmed: 21799992
Mei J, Hong Y, Lam JWY, Qin A, Tang Y, Tang BZ (2014) Aggregation-induced emission: the whole is more brilliant than the parts. Adv Mater 26:5429–5479
doi: 10.1002/adma.201401356
pubmed: 24975272
Leung NL, Xie N, Yuan W, Liu Y, Wu Q, Peng Q, Miao Q, Lam JW, Tang BZ (2014) Restriction of intramolecular motions: the general mechanism behind aggregation-induced emission. Chemistry (Easton) 20:15349–15353
Liu Y, Yu Y, Lam JWY, Hong Y, Faisal M, Yuan WZ, Tang BZ (2010) Simple biosensor with high selectivity and sensitivity: thiol-specific biomolecular probing and intracellular imaging by AIE fluorogen on a TLC plate through a thiol–Ene click mechanism. Chem Eur J 16:8433–8438
doi: 10.1002/chem.200902505
pubmed: 20544746
Zhang S, Liu M, Tan LYF, Hong Q, Pow ZL, Owyong TC, Ding S, Wong WWH, Hong Y (2019) A Maleimide-functionalized tetraphenylethene for measuring and imaging unfolded proteins in cells. Chem Asian J 14:904–909
doi: 10.1002/asia.201900150
pubmed: 30768765
Owyong TC, Subedi P, Deng J, Hinde E, Paxman JJ, White JM, Chen W, Heras B, Wong WWH, Hong Y (2019) A molecular chameleon for mapping subcellular polarity in an unfolded proteome environment. Angew Chem Int Ed Engl
Klymchenko AS (2017) Solvatochromic and fluorogenic dyes as environment-sensitive probes: design and biological applications. Acc Chem Res 50:366–375
doi: 10.1021/acs.accounts.6b00517
pubmed: 28067047
McKinnon KM (2018) Flow cytometry: an overview. Curr Protoc Immunol 120:5.1.1–5.1.11
doi: 10.1002/cpim.40
Rigby PJ, Goldie RG (1999) Confocal microscopy in biomedical research. Croat Med J 40:346–352
pubmed: 10411961
Parakh S, Shadfar S, Perri ER, Ragagnin AMG, Piattoni CV, Fogolín MB, Yuan KC, Shahheydari H, Don EK, Thomas CJ, Hong Y, Comini MA, Laird AS, Spencer DM, Atkin JD (2020) The redox activity of protein disulfide isomerase inhibits ALS phenotypes in cellular and zebrafish models. iScience 23:101097
doi: 10.1016/j.isci.2020.101097
pubmed: 32446203
pmcid: 7240177
Hidalgo San Jose L, Sunshine MJ, Dillingham CH, Chua BA, Kruta M, Hong Y, Hatters DM, Signer RAJ (2020) Modest declines in proteome quality impair hematopoietic stem cell self-renewal. Cell Rep 30:69–80.e66
doi: 10.1016/j.celrep.2019.12.003
pubmed: 31914399
Hu D, Sun X, Liao X, Zhang X, Zarabi S, Schimmer A, Hong Y, Ford C, Luo Y, Qi X (2019) Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity. Acta Neuropathol 137:939–960
doi: 10.1007/s00401-019-01993-2
pubmed: 30877431
pmcid: 6531426
Brocchieri L, Karlin S (2005) Protein length in eukaryotic and prokaryotic proteomes. Nucleic Acids Res 33:3390–3400
doi: 10.1093/nar/gki615
pubmed: 15951512
pmcid: 1150220