UCHL1 Promoted Polarization of M1 Macrophages by Regulating the PI3K/AKT Signaling Pathway

References

• Phan AT, Goldrath AW, Glass CK. Metabolic and epigenetic coordination of T cell and macrophage immunity. Immunity. 2017;46(5):714–729. doi:10.1016/j.immuni.2017.04.016
   PubMed Web of Science ®Google Scholar
• Ginhoux F, Schultze JL, Murray PJ, Ochando J, Biswas SK. New insights into the multidimensional concept of macrophage ontogeny, activation and function. Nat Immunol. 2016;17(1):34–40. doi:10.1038/ni.3324
   PubMed Web of Science ®Google Scholar
• Wynn TA, Chawla A, Pollard JW. Macrophage biology in development, homeostasis and disease. Nature. 2013;496(7446):445–455. doi:10.1038/nature12034
   PubMed Web of Science ®Google Scholar
• Murray PJ. Macrophage polarization. Annu Rev Physiol. 2017;79(1):541–566. doi:10.1146/annurev-physiol-022516-034339
   PubMed Web of Science ®Google Scholar
• Kimura T, Nada S, Takegahara N, et al. Polarization of M2 macrophages requires Lamtor1 that integrates cytokine and amino-acid signals. Nat Commun. 2016;7(1):13130. doi:10.1038/ncomms13130
   PubMed Web of Science ®Google Scholar
• Franke TF, Yang SI, Chan TO, et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 1995;81(5):727–736. doi:10.1016/0092-8674(95)90534-0
   PubMed Web of Science ®Google Scholar
• Song G, Ouyang G, Bao S. The activation of Akt/PKB signaling pathway and cell survival. J Cell Mol Med. 2005;9(1):59–71. doi:10.1111/j.1582-4934.2005.tb00337.x
   PubMed Web of Science ®Google Scholar
• Franke TF. PI3K/Akt: getting it right matters. Oncogene. 2008;27(50):6473–6488. doi:10.1038/onc.2008.313
   PubMed Web of Science ®Google Scholar
• Gao T, Furnari F, Newton AC. PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol Cell. 2005;18(1):13–24. doi:10.1016/j.molcel.2005.03.008
   PubMed Web of Science ®Google Scholar
• Beaulieu JM, Sotnikova TD, Marion S, Lefkowitz RJ, Gainetdinov RR, Caron MG. An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell. 2005;122(2):261–273. doi:10.1016/j.cell.2005.05.012
   PubMed Web of Science ®Google Scholar
• Maira SM, Galetic I, Brazil DP, et al. Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane. Science. 2001;294(5541):374–380. doi:10.1126/science.1062030
   PubMed Web of Science ®Google Scholar
• Geering B, Cutillas PR, Nock G, Gharbi SI, Vanhaesebroeck B. Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers. Proc Natl Acad Sci USA. 2007;104:7809–7814.
   PubMed Web of Science ®Google Scholar
• Kok K, Geering B, Vanhaesebroeck B. Regulation of phosphoinositide 3-kinase expression in health and disease. Trends Biochem Sci. 2009;34(3):115–127. doi:10.1016/j.tibs.2009.01.003
   PubMed Web of Science ®Google Scholar
• Engelman JA. Targeting PI3K signalling in cancer: opportunities, challenges and limitations. Nat Rev Cancer. 2009;9(8):550–562. doi:10.1038/nrc2664
   PubMed Web of Science ®Google Scholar
• Yuan TL, Cantley LC. PI3K pathway alterations in cancer: variations on a theme. Oncogene. 2008;27(41):5497–5510. doi:10.1038/onc.2008.245
   PubMed Web of Science ®Google Scholar
• Samuels Y, Wang Z, Bardelli A, et al. High frequency of mutations of the PIK3CA gene in human cancers. Science. 2004;304:554. doi:10.1126/science.1096502
   PubMed Web of Science ®Google Scholar
• Yuan TL, Wulf G, Burga L, Cantley LC. Cell-to-cell variability in PI3K protein level regulates PI3K-AKT pathway activity in cell populations. Curr Biol. 2011;21(3):173–183. doi:10.1016/j.cub.2010.12.047
   PubMed Web of Science ®Google Scholar
• Hu H, Sun SC. Ubiquitin signaling in immune responses. Cell Res. 2016;26(4):457–483. doi:10.1038/cr.2016.40
   PubMed Web of Science ®Google Scholar
• Fu Y, Wang P, Zhao J, et al. USP12 promotes CD4(+) T cell responses through deubiquitinating and stabilizing BCL10. Cell Death Differ. 2021;28(10):2857–2870. doi:10.1038/s41418-021-00787-y
   PubMed Web of Science ®Google Scholar
• Jarome TJ, Devulapalli RK. The ubiquitin-proteasome system and memory: moving beyond protein degradation. Neuroscientist. 2018;24(6):639–651. doi:10.1177/1073858418762317
   PubMed Web of Science ®Google Scholar
• Varshavsky A. The ubiquitin system, autophagy, and regulated protein degradation. Annu Rev Biochem. 2017;86(1):123–128. doi:10.1146/annurev-biochem-061516-044859
   PubMed Web of Science ®Google Scholar
• Kulathu Y, Komander D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol. 2012;13(8):508–523. doi:10.1038/nrm3394
   PubMed Web of Science ®Google Scholar
• Sun SC. Deubiquitylation and regulation of the immune response. Nat Rev Immunol. 2008;8(7):501–511. doi:10.1038/nri2337
   PubMed Web of Science ®Google Scholar
• Wertz IE, Wang X. From discovery to bedside: targeting the ubiquitin system. Cell Chem Biol. 2019;26(2):156–177. doi:10.1016/j.chembiol.2018.10.022
   PubMed Web of Science ®Google Scholar
• Bedford L, Lowe J, Dick LR, Mayer RJ, Brownell JE. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov. 2011;10(1):29–46. doi:10.1038/nrd3321
   PubMed Web of Science ®Google Scholar
• Doran JF, Jackson P, Kynoch PA, Thompson RJ. Isolation of PGP 9.5, a new human neurone-specific protein detected by high-resolution two-dimensional electrophoresis. J Neurochem. 1983;40(6):1542–1547. doi:10.1111/j.1471-4159.1983.tb08124.x
   PubMed Web of Science ®Google Scholar
• Liu Y, Fallon L, Lashuel HA, Liu Z, Lansbury PT Jr. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility. Cell. 2002;111(2):209–218. doi:10.1016/S0092-8674(02)01012-7
   PubMed Web of Science ®Google Scholar
• Larsen CN, Krantz BA, Wilkinson KD. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry. 1998;37:3358–3368.
   PubMed Web of Science ®Google Scholar
• Wilkinson KD, Lee KM, Deshpande S, Duerksen-Hughes P, Boss JM, Pohl J. The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science. 1989;246(4930):670–673. doi:10.1126/science.2530630
   PubMed Web of Science ®Google Scholar
• Lunati A, Lesage S, Brice A. The genetic landscape of Parkinson’s disease. Rev Neurol. 2018;174(9):628–643. doi:10.1016/j.neurol.2018.08.004
   PubMed Web of Science ®Google Scholar
• Tramutola A, Di Domenico F, Barone E, Perluigi M, Butterfield DA. It is all about (U)biquitin: role of altered ubiquitin-proteasome system and UCHL1 in Alzheimer disease. Oxid Med Cell Longev. 2016;2016:2756068. doi:10.1155/2016/2756068
   PubMed Web of Science ®Google Scholar
• Wang KK, Yang Z, Zhu T, et al. An update on diagnostic and prognostic biomarkers for traumatic brain injury. Expert Rev Mol Diagn. 2018;18(2):165–180. doi:10.1080/14737159.2018.1428089
   PubMed Web of Science ®Google Scholar
• Zhang Y, Fan Y, Jing X, et al. OTUD5-mediated deubiquitination of YAP in macrophage promotes M2 phenotype polarization and favors triple-negative breast cancer progression. Cancer Lett. 2021;504:104–115. doi:10.1016/j.canlet.2021.02.003
   PubMed Web of Science ®Google Scholar
• Xu F, Ma Y, Huang W, et al. Typically inhibiting USP14 promotes autophagy in M1-like macrophages and alleviates CLP-induced sepsis. Cell Death Dis. 2020;11(8):666. doi:10.1038/s41419-020-02898-9
   PubMed Web of Science ®Google Scholar
• Liu T, Wang L, Liang P, et al. USP19 suppresses inflammation and promotes M2-like macrophage polarization by manipulating NLRP3 function via autophagy. Cell Mol Immunol. 2020;18(10):2431–2442.
   PubMed Web of Science ®Google Scholar
• Lin X, Zhang H, Boyce BF, Xing L. Ubiquitination of interleukin-1α is associated with increased pro-inflammatory polarization of murine macrophages deficient in the E3 ligase ITCH. J Biol Chem. 2020;295(33):11764–11775. doi:10.1074/jbc.RA120.014298
   PubMed Web of Science ®Google Scholar
• Zhao X, Huang XH, Dong XH, et al. Deubiquitinase Mysm1 regulates macrophage survival and polarization. Mol Biol Rep. 2018;45(6):2393–2401. doi:10.1007/s11033-018-4405-3
   PubMed Web of Science ®Google Scholar
• Day IN, Thompson RJ. UCHL1 (PGP 9.5): neuronal biomarker and ubiquitin system protein. Prog Neurobiol. 2010;90(3):327–362. doi:10.1016/j.pneurobio.2009.10.020
   PubMed Web of Science ®Google Scholar
• Hussain S, Bedekovics T, Ali A, et al. A cysteine near the C-terminus of UCH-L1 is dispensable for catalytic activity but is required to promote AKT phosphorylation, eIF4F assembly, and malignant B-cell survival. Cell Death Discov. 2019;5(1):152. doi:10.1038/s41420-019-0231-1
   PubMed Web of Science ®Google Scholar
• Luo Y, He J, Yang C, et al. UCH-L1 promotes invasion of breast cancer cells through activating Akt signaling pathway. J Cell Biochem. 2018;119(1):691–700. doi:10.1002/jcb.26232
   PubMed Web of Science ®Google Scholar
• Jin Y, Zhou H, Gong L, Xia J, Yu G, Chen Y. Prognostic potential and oncogenic effects of UCH-L1 expression in hilar cholangiocarcinoma. Int J Clin Exp Pathol. 2017;10(11):10802–10811.
   PubMed Web of Science ®Google Scholar
• Gu YY, Yang M, Zhao M, et al. The de-ubiquitinase UCHL1 promotes gastric cancer metastasis via the Akt and Erk1/2 pathways. Tumour Biol. 2015;36(11):8379–8387. doi:10.1007/s13277-015-3566-0
   PubMedGoogle Scholar
• Hussain S, Feldman AL, Das C, Ziesmer SC, Ansell SM, Galardy PJ. Ubiquitin hydrolase UCH-L1 destabilizes mTOR complex 1 by antagonizing DDB1-CUL4-mediated ubiquitination of raptor. Mol Cell Biol. 2013;33(6):1188–1197. doi:10.1128/MCB.01389-12
   PubMed Web of Science ®Google Scholar
• Karim R, Tummers B, Meyers C, et al. Human papillomavirus (HPV) upregulates the cellular deubiquitinase UCHL1 to suppress the keratinocyte’s innate immune response. PLoS Pathog. 2013;9(5):e1003384. doi:10.1371/journal.ppat.1003384
   PubMed Web of Science ®Google Scholar
• Hussain S, Foreman O, Perkins SL, et al. The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling. Leukemia. 2010;24(9):1641–1655. doi:10.1038/leu.2010.138
   PubMed Web of Science ®Google Scholar
• Mitra S, Sammani S, Wang T, et al. Role of growth arrest and DNA damage-inducible α in Akt phosphorylation and ubiquitination after mechanical stress-induced vascular injury. Am J Respir Crit Care Med. 2011;184(9):1030–1040. doi:10.1164/rccm.201103-0447OC
   PubMed Web of Science ®Google Scholar