Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities
Abstract
:Simple Summary
Abstract
1. Introduction
2. The Discovery and Study of Proline Isomerization in History: From Initial Observations to Modern Insights
3. Proline Isomerization Catalyzers: Peptidyl-Prolyl Isomerases
3.1. Cyclophilins
3.2. FK506 Binding Proteins (FKBPs)
3.3. Parvulins
4. Tying It Altogether: Showcase of Proline Isomerization as a Regulatory Mechanism in Cellular Response and Function
4.1. ATR Is Regulated by Proline Isomerization to Switch between Its Dual Role in Modulating Cell Death and DNA Damage Checkpoint Signaling
4.2. p53 Is Regulated by Proline Isomerization at Multiple Sites in Response to DNA Repair and Cellular Stress, Respectively
4.3. Itk Is Activated by Proline Isomerization in T-Cells
4.4. The Gate Function of 5-HT3 Receptor Is Regulated by Proline Isomerization
5. Role of Proline Isomerization in Human Disease
5.1. Autoimmune Disease
5.2. Cancer
5.3. Infectious Disease
5.4. Neurodegenerative Disease
6. Prolyl Isomerase Inhibitors
6.1. Cyclophilin Inhibitors
6.2. FKBP Inhibitors
6.3. Pin1 Inhibitors
7. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Prolyl Isomerase | Protein Size | Preferred Proline Site | Triggers | Substrate Proteins | Subcellular Localization |
---|---|---|---|---|---|
FK506 binding proteins | 12–52 kDa | Xaa-Pro | Ligand binding, change in local environment of the protein such as pH | Tau APP, ryanodine receptor, Inositol 1,4,5-triphosphate receptor, TGF-β, heat-shock proteins, nuclear transport receptor including androgen receptor | Cytoplasm (primary), endoplasm reticulum (ER), and nucleus |
Cyclophilins | 18–45 kDa | Xaa-Pro | Ligand binding, change in local environment of the protein such as pH | HIV1 capsid, NS5A of hepatitis C virus, heat -shock proteins (HSP90), α-synuclein | Cytosol, ER, mitochondria and nucleus |
Parvulins | 14, 17, and 18 kDa | pSer/pThr-Pro (Pin1) Arg/Leu-Pro (Par14 and Par17) | Phosphorylation on Ser or Thr proceeding to Pro residue (Pin1) Arginine or leucine residues (Par14 and Par17) | ATR, p53, CDC25, α-synuclein, survivin, β-catenin, NF-kβ, Cyclin D1, C-Jun, RNA pol II | Nucleus (Pin1) Nucleus and cytosol (Par14) Mitochondria (Par17) |
Inhibitors | Inhibitor Target | IC50 or Ki | Inhibitor Type | Reference |
---|---|---|---|---|
Cyclosporine | Cyclophilins | 420 ± 56 nM | Immunosuppressive | Sedrani et al., 2003 [226] |
Debio-025 | 0.18 ± 0.03 nM | Non-Immunosuppressive Cyclosporine analog | Ptak et al., 2008 [227], Paeshuyse et al., 2006 [228] | |
NIM811 | 0.66 μM | Non-Immunosuppressive Cyclosporine analog | Ma et al., 2006 [229] | |
CRV431 | 2.5 nM (CypA) | Non-Immunosuppressive Cyclosporine analog | Kuo et al., 2019 [230] | |
SCY-635 | 1.84 μM | Non-Immunosuppressive Cyclosporine analog | Hopkins et al., 2010 [231] | |
Sanglifehrin A | 6.9 ± 0.9 nM | Immunosuppressive Sanglifehrin | Sedrani et al., 2003 [226] | |
NV651 | 6.3 nM | Non-Immunosuppressive Sanglifehrin analog | Serrano et al., 2021 [232] | |
NV556 | Non-Immunosuppressive Sanglifehrin analog | Kuo et al., 2019 [230], Serrano et al., 2019 [233] | ||
Rapamycin | FKBPs | 0.1 nM | Immunosuppressive | Kolos et al., 2018 [61] |
FK506 | 1 nM | Immunosuppressive | Kolos et al., 2018 [61] | |
GPI-1485 | Immunosuppressive | Kolos et al., 2018 [61] | ||
SaFit1 | 4 nM | Non-Immunosuppressive | Gaali et al., 2015 [234] | |
SaFit2 | 8 nM | Non-Immunosuppressive | Gaali et al., 2015 [234] | |
Juglone | Pin1 | 7.68 μM | Covalent inhibitor | Zhang et al., 2015 [235] |
KPT-6566 | 0.64 μM | Covalent inhibitor | Campaner et al., 2017 [236] | |
(S)-2 | 3.2 μM | Covalent inhibitor | Ieda et al., 2010 [237] | |
BJP-06-005-3 | 48 nM | Non-covalent inhibitor | Pinch et al., 2020 [238] | |
ZL-Pin13 | 0.067 ± 0.03 μM | Covalent inhibitor | Liu et al., 2022 [239] | |
Sulfopin | 38 nM | Covalent inhibitor | Dubiella et al., 2021 [240] | |
D-PEPTIDE | 20.4 ± 4.3 nM | Non-covalent inhibitor | Zhang et al., 2007 [55] | |
Compound 21b | 6 nM | Non-covalent inhibitor | Guo et al., 2009 [241] | |
Compound 23b | 890 nM | Non-covalent inhibitor | Dong et al., 2010 [242] | |
Compound 22C | 196 nM | Non-covalent inhibitor | Guo et al., 2014 [243] | |
VS1 | >100 μM | Non-covalent inhibitor | Poli et al., 2022 [244] | |
VS2 | 19 ± 3 μM | Non-covalent inhibitor | Poli et al., 2022 [244] | |
ATRA | 112 ± 10 μM | Non-covalent inhibitor | Poli et al., 2022 [244] |
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Gurung, D.; Danielson, J.A.; Tasnim, A.; Zhang, J.-T.; Zou, Y.; Liu, J.-Y. Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities. Biology 2023, 12, 1008. https://doi.org/10.3390/biology12071008
Gurung D, Danielson JA, Tasnim A, Zhang J-T, Zou Y, Liu J-Y. Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities. Biology. 2023; 12(7):1008. https://doi.org/10.3390/biology12071008
Chicago/Turabian StyleGurung, Deepti, Jacob A Danielson, Afsara Tasnim, Jian-Ting Zhang, Yue Zou, and Jing-Yuan Liu. 2023. "Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities" Biology 12, no. 7: 1008. https://doi.org/10.3390/biology12071008
APA StyleGurung, D., Danielson, J. A., Tasnim, A., Zhang, J. -T., Zou, Y., & Liu, J. -Y. (2023). Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities. Biology, 12(7), 1008. https://doi.org/10.3390/biology12071008