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Journal articles on the topic 'Peptidyl-prolyl cis/trans isomérase'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Lavoie, Sébastien B., Alexandra L. Albert, and Michel Vincent. "Pin1 : une peptidyl-prolyl cis/trans isomérase aux rôles insoupçonnés." médecine/sciences 19, no. 12 (December 2003): 1251–58. http://dx.doi.org/10.1051/medsci/200319121251.

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2

Schiene-Fischer, Cordelia. "Multidomain Peptidyl Prolyl cis/trans Isomerases." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 10 (October 2015): 2005–16. http://dx.doi.org/10.1016/j.bbagen.2014.11.012.

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3

Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases (PPIases)." Frontiers in Bioscience 5, no. 1 (2000): d821. http://dx.doi.org/10.2741/maruyama.

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4

Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases PPIases." Frontiers in Bioscience 5, no. 3 (2000): d821–836. http://dx.doi.org/10.2741/a554.

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5

Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004." Frontiers in Bioscience 9, no. 1-3 (2004): 1680. http://dx.doi.org/10.2741/1361.

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6

Schiene, Cordelia, Ulf Reimer, Mike Schutkowski, and Gunter Fischer. "Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases." FEBS Letters 432, no. 3 (August 7, 1998): 202–6. http://dx.doi.org/10.1016/s0014-5793(98)00871-0.

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7

Yli-Kauhaluoma, Jari T., Jon A. Ashley, Chih-Hung L. Lo, Julie Coakley, Peter Wirsching, and Kim D. Janda. "Catalytic Antibodies with Peptidyl−Prolyl Cis−Trans Isomerase Activity." Journal of the American Chemical Society 118, no. 23 (January 1996): 5496–97. http://dx.doi.org/10.1021/ja954206p.

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8

Caporale, Andrea, Fabiola Mascanzoni, Biancamaria Farina, Mattia Sturlese, Gianluigi Di Sorbo, Roberto Fattorusso, Menotti Ruvo, and Nunzianna Doti. "FRET-Protease-Coupled Peptidyl-Prolyl cis-trans Isomerase Assay." Journal of Biomolecular Screening 21, no. 7 (July 10, 2016): 701–12. http://dx.doi.org/10.1177/1087057116650402.

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In this work, a sensitive and convenient protease-based fluorimetric high-throughput screening (HTS) assay for determining peptidyl-prolyl cis-trans isomerase activity was developed. The assay was based on a new intramolecularly quenched substrate, whose fluorescence and structural properties were examined together with kinetic constants and the effects of solvents on its isomerization process. Pilot screens performed using the Library of Pharmacologically Active Compounds (LOPAC) and cyclophilin A (CypA), as isomerase model enzyme, indicated that the assay was robust for HTS, and that comparable results were obtained with a CypA inhibitor tested both manually and automatically. Moreover, a new compound that inhibits CypA activity with an IC50 in the low micromolar range was identified. Molecular docking studies revealed that the molecule shows a notable shape complementarity with the catalytic pocket confirming the experimental observations. Due to its simplicity and precision in the determination of extent of inhibition and reaction rates required for kinetic analysis, this assay offers many advantages over other commonly used assays.

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9

Hassidim, Miriam, Rakefet Schwarz, Judy Lieman-Hurwitz, Eduardo Marco, Michal Ronen-Tarazi, and Aaron Kaplan. "A Cyanobacterial Gene Encoding Peptidyl-Prolyl cis-trans Isomerase." Plant Physiology 100, no. 4 (December 1, 1992): 1982–86. http://dx.doi.org/10.1104/pp.100.4.1982.

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10

Ruddock, Lloyd. "Peptidyl-Prolyl Cis/Trans Isomerases. Andrzej Galat , Sylvie Riviere." Quarterly Review of Biology 75, no. 3 (September 2000): 312–13. http://dx.doi.org/10.1086/393523.

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11

Reimer, Ulf, Gerd Scherer, Mario Drewello, Susanne Kruber, Mike Schutkowski, and Gunter Fischer. "Side-chain effects on peptidyl-prolyl cis/trans isomerisation." Journal of Molecular Biology 279, no. 2 (June 1998): 449–60. http://dx.doi.org/10.1006/jmbi.1998.1770.

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12

Fischer, Gunter. "Über Peptidyl-Prolyl-cis/trans-Isomerasen und ihre Effektoren." Angewandte Chemie 106, no. 14 (July 14, 1994): 1479–501. http://dx.doi.org/10.1002/ange.19941061404.

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13

Galat, Andrzej. "Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series." Biomolecules 9, no. 2 (February 20, 2019): 74. http://dx.doi.org/10.3390/biom9020074.

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About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]

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14

Hidaka, Masafumi, Keita Kosaka, Saori Tsushima, Chiyoko Uchida, Katsuhiko Takahashi, Noriko Takahashi, Masayoshi Tsubuki, Yukihiko Hara, and Takafumi Uchida. "Food polyphenols targeting peptidyl prolyl cis/trans isomerase Pin1." Biochemical and Biophysical Research Communications 499, no. 3 (May 2018): 681–87. http://dx.doi.org/10.1016/j.bbrc.2018.03.212.

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15

Paillares, Eléa, Maud Marechal, Léa Swistak, Landry Tsoumtsa Meda, Emmanuel Lemichez, and Thérèse E. Malliavin. "Conformational Insights into the Control of CNF1 Toxin Activity by Peptidyl-Prolyl Isomerization: A Molecular Dynamics Perspective." International Journal of Molecular Sciences 22, no. 18 (September 20, 2021): 10129. http://dx.doi.org/10.3390/ijms221810129.

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The cytotoxic necrotizing factor 1 (CNF1) toxin from uropathogenic Escherichia coli constitutively activates Rho GTPases by catalyzing the deamidation of a critical glutamine residue located in the switch II (SWII). In crystallographic structures of the CNF1 catalytic domain (CNF1CD), surface-exposed P768 and P968 peptidyl-prolyl imide bonds (X-Pro) adopt an unusual cis conformation. Here, we show that mutation of each proline residue into glycine abrogates CNF1CD in vitro deamidase activity, while mutant forms of CNF1 remain functional on RhoA in cells. Using molecular dynamics simulations coupled to protein-peptide docking, we highlight the long-distance impact of peptidyl-prolyl cis-trans isomerization on the network of interactions between the loops bordering the entrance of the catalytic cleft. The energetically favorable isomerization of P768 compared with P968, induces an enlargement of loop L1 that fosters the invasion of CNF1CD catalytic cleft by a peptide encompassing SWII of RhoA. The connection of the P968 cis isomer to the catalytic cysteine C866 via a ladder of stacking interactions is alleviated along the cis-trans isomerization. Finally, the cis-trans conversion of P768 favors a switch of the thiol side chain of C866 from a resting to an active orientation. The long-distance impact of peptidyl-prolyl cis-trans isomerizations is expected to have implications for target modification.

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16

Kromina, K. A., A. N. Ignatov, and I. A. Abdeeva. "Role of peptidyl-prolyl-cis/trans-isomerases in pathologic processes." Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology 2, no. 3 (August 29, 2008): 195–202. http://dx.doi.org/10.1134/s199074780803001x.

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17

FISCHER, G. "ChemInform Abstract: Peptidyl-Prolyl cis/trans Isomerases and Their Effectors." ChemInform 25, no. 50 (August 18, 2010): no. http://dx.doi.org/10.1002/chin.199450303.

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18

Ahmad, Saleem, Sen Wang, Weizhong Wu, Kunlong Yang, YanFeng Zhang, Elisabeth Tumukunde, Shihua Wang, and Yu Wang. "Functional Analysis of Peptidyl-prolyl cis-trans Isomerase from Aspergillus flavus." International Journal of Molecular Sciences 20, no. 9 (May 5, 2019): 2206. http://dx.doi.org/10.3390/ijms20092206.

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Aspergillus flavus, a ubiquitous filamentous fungus found in soil, plants and other substrates has been reported not only as a pathogen for plants, but also a carcinogen producing fungus for human. Peptidyl-Prolyl Isomerase (PPIases) plays an important role in cell process such as protein secretion cell cycle control and RNA processing. However, the function of PPIase has not yet been identified in A. flavus. In this study, the PPIases gene from A. flavus named ppci1 was cloned into expression vector and the protein was expressed in prokaryotic expression system. Activity of recombinant ppci1 protein was particularly inhibited by FK506, CsA and rapamycin. 3D-Homology model of ppci1 has been constructed with the template, based on 59.7% amino acid similarity. The homologous recombination method was used to construct the single ppci1 gene deletion strain Δppci1. We found that, the ppci1 gene plays important roles in A. flavus growth, conidiation, and sclerotia formation, all of which showed reduction in Δppci1 and increased in conidiation compared with the wild-type and complementary strains in A. flavus. Furthermore, aflatoxin and peanut seeds infection assays indicated that ppci1 contributes to virulence of A. flavus. Furthermore, we evaluated the effect of PPIase inhibitors on A. flavus growth, whereby these were used to treat wild-type strains. We found that the growths were inhibited under every inhibitor. All, these results may provide valuable information for designing inhibitors in the controlling infections of A. flavus.

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19

FanghÃ¤nel, JÃ¶rg. "Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases." Frontiers in Bioscience 9, no. 1-3 (2004): 3453. http://dx.doi.org/10.2741/1494.

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20

Wang, M. L., W. J. Li, and W. B. Xu. "Support vector machines for prediction of peptidyl prolyl cis/trans isomerization." Journal of Peptide Research 63, no. 1 (December 5, 2008): 23–28. http://dx.doi.org/10.1046/j.1399-3011.2004.00100.x.

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21

Fischer, Gunter, Brigitte Wittmann-Liebold, Kurt Lang, Thomas Kiefhaber, and Franz X. Schmid. "Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins." Nature 337, no. 6206 (February 1989): 476–78. http://dx.doi.org/10.1038/337476a0.

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22

Garcia-Echeverria, Carlos, James L. Kofron, Petr Kuzmic, Vimal Kishore, and Daniel H. Rich. "Continuous fluorimetric direct (uncoupled) assay for peptidyl prolyl cis-trans isomerases." Journal of the American Chemical Society 114, no. 7 (March 1992): 2758–59. http://dx.doi.org/10.1021/ja00033a083.

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23

Daum, Sebastian, Frank Erdmann, Gunter Fischer, Boris Féaux de Lacroix, Anahita Hessamian-Alinejad, Sabine Houben, Walter Frank, and Manfred Braun. "Arylindanylketone: effiziente Inhibitoren der humanen Peptidyl-Prolyl-cis/trans-Isomerase Pin1." Angewandte Chemie 118, no. 44 (November 13, 2006): 7615–19. http://dx.doi.org/10.1002/ange.200601569.

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24

Maelicke, Alfred. "Peptidyl-prolyl-cis-trans Isomerase und die Aktivierung von T-Lymphocyten." Nachrichten aus Chemie, Technik und Laboratorium 37, no. 12 (December 1989): 1299–300. http://dx.doi.org/10.1002/nadc.19890371211.

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25

Garciaecheverria, C., J. L. Kofron, P. Kuzmic, and D. H. Rich. "A Continuous Spectrophotometric Direct Assay for Peptidyl Prolyl cis-trans Isomerases." Biochemical and Biophysical Research Communications 191, no. 1 (February 1993): 70–75. http://dx.doi.org/10.1006/bbrc.1993.1185.

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26

Erben, Esteban D., Ezequiel Valguarnera, Sheila Nardelli, Janete Chung, Sebastian Daum, Mariana Potenza, Sergio Schenkman, and María T. Téllez-Iñón. "Identification of an atypical peptidyl-prolyl cis/trans isomerase from trypanosomatids." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1803, no. 9 (September 2010): 1028–37. http://dx.doi.org/10.1016/j.bbamcr.2010.05.006.

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27

G�thel, S. F., and M. A. Marahiel. "Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts." Cellular and Molecular Life Sciences (CMLS) 55, no. 3 (March 1, 1999): 423–36. http://dx.doi.org/10.1007/s000180050299.

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28

Troilo, Francesca, Francesca Malagrinò, Lorenzo Visconti, Angelo Toto, and Stefano Gianni. "The Effect of Proline cis-trans Isomerization on the Folding of the C-Terminal SH2 Domain from p85." International Journal of Molecular Sciences 21, no. 1 (December 23, 2019): 125. http://dx.doi.org/10.3390/ijms21010125.

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SH2 domains are protein domains that modulate protein–protein interactions through a specific interaction with sequences containing phosphorylated tyrosines. In this work, we analyze the folding pathway of the C-terminal SH2 domain of the p85 regulatory subunit of the protein PI3K, which presents a proline residue in a cis configuration in the loop between the βE and βF strands. By employing single and double jump folding and unfolding experiments, we demonstrate the presence of an on-pathway intermediate that transiently accumulates during (un)folding. By comparing the kinetics of folding of the wild-type protein to that of a site-directed variant of C-SH2 in which the proline was replaced with an alanine, we demonstrate that this intermediate is dictated by the peptidyl prolyl cis-trans isomerization. The results are discussed in the light of previous work on the effect of peptidyl prolyl cis-trans isomerization on folding events.

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29

Hasel, K. W., J. R. Glass, M. Godbout, and J. G. Sutcliffe. "An endoplasmic reticulum-specific cyclophilin." Molecular and Cellular Biology 11, no. 7 (July 1991): 3484–91. http://dx.doi.org/10.1128/mcb.11.7.3484.

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Cyclophilin is a ubiquitously expressed cytosolic peptidyl-prolyl cis-trans isomerase that is inhibited by the immunosuppressive drug cyclosporin A. A degenerate oligonucleotide based on a conserved cyclophilin sequence was used to isolate cDNA clones representing a ubiquitously expressed mRNA from mice and humans. This mRNA encodes a novel 20-kDa protein, CPH2, that shares 64% sequence identity with cyclophilin. Bacterially expressed CPH2 binds cyclosporin A and is a cyclosporin A-inhibitable peptidyl-prolyl cis-trans isomerase. Cell fractionation of rat liver followed by Western blot (immunoblot) analysis indicated that CPH2 is not cytosolic but rather is located exclusively in the endoplasmic reticulum. These results suggest that cyclosporin A mediates its effect on cells through more than one cyclophilin and that cyclosporin A-induced misfolding of T-cell membrane proteins normally mediated by CPH2 plays a role in immunosuppression.

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30

Hasel, K. W., J. R. Glass, M. Godbout, and J. G. Sutcliffe. "An endoplasmic reticulum-specific cyclophilin." Molecular and Cellular Biology 11, no. 7 (July 1991): 3484–91. http://dx.doi.org/10.1128/mcb.11.7.3484-3491.1991.

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Cyclophilin is a ubiquitously expressed cytosolic peptidyl-prolyl cis-trans isomerase that is inhibited by the immunosuppressive drug cyclosporin A. A degenerate oligonucleotide based on a conserved cyclophilin sequence was used to isolate cDNA clones representing a ubiquitously expressed mRNA from mice and humans. This mRNA encodes a novel 20-kDa protein, CPH2, that shares 64% sequence identity with cyclophilin. Bacterially expressed CPH2 binds cyclosporin A and is a cyclosporin A-inhibitable peptidyl-prolyl cis-trans isomerase. Cell fractionation of rat liver followed by Western blot (immunoblot) analysis indicated that CPH2 is not cytosolic but rather is located exclusively in the endoplasmic reticulum. These results suggest that cyclosporin A mediates its effect on cells through more than one cyclophilin and that cyclosporin A-induced misfolding of T-cell membrane proteins normally mediated by CPH2 plays a role in immunosuppression.

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31

Jiang, Quan, Xiao-Rong Li, Cheng-Kun Wang, Juan Cheng, Chao Tan, Tian-Tian Cui, Nan-Nan Lu, Tony D. James, Feng Han, and Xin Li. "A fluorescent peptidyl substrate for visualizing peptidyl-prolyl cis/trans isomerase activity in live cells." Chemical Communications 54, no. 15 (2018): 1857–60. http://dx.doi.org/10.1039/c7cc09135d.

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32

Barth, Sandra, Jutta Nesper, Philippe A. Hasgall, Renato Wirthner, Katarzyna J. Nytko, Frank Edlich, Dörthe M. Katschinski, Daniel P. Stiehl, Roland H. Wenger, and Gieri Camenisch. "The Peptidyl Prolyl cis/trans Isomerase FKBP38 Determines Hypoxia-Inducible Transcription Factor Prolyl-4-Hydroxylase PHD2 Protein Stability." Molecular and Cellular Biology 27, no. 10 (March 12, 2007): 3758–68. http://dx.doi.org/10.1128/mcb.01324-06.

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ABSTRACT The heterodimeric hypoxia-inducible transcription factors (HIFs) are central regulators of the response to low oxygenation. HIF-α subunits are constitutively expressed but rapidly degraded under normoxic conditions. Oxygen-dependent hydroxylation of two conserved prolyl residues by prolyl-4-hydroxylase domain-containing enzymes (PHDs) targets HIF-α for proteasomal destruction. We identified the peptidyl prolyl cis/trans isomerase FK506-binding protein 38 (FKBP38) as a novel interactor of PHD2. Yeast two-hybrid, glutathione S-transferase pull-down, coimmunoprecipitation, colocalization, and mammalian two-hybrid studies confirmed specific FKBP38 interaction with PHD2, but not with PHD1 or PHD3. PHD2 and FKBP38 associated with their N-terminal regions, which contain no known interaction motifs. Neither FKBP38 mRNA nor protein levels were regulated under hypoxic conditions or after PHD inhibition, suggesting that FKBP38 is not a HIF/PHD target. Stable RNA interference-mediated depletion of FKBP38 resulted in increased PHD hydroxylation activity and decreased HIF protein levels and transcriptional activity. Reconstitution of FKBP38 expression abolished these effects, which were independent of the peptidyl prolyl cis/trans isomerase activity. Downregulation of FKBP38 did not affect PHD2 mRNA levels but prolonged PHD2 protein stability, suggesting that FKBP38 is involved in PHD2 protein regulation.

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33

Bennett, Pauleen C., Lloyd G. Singaretnam, Wei-Qin Zhao, Alfons Lawen, and Kim T. Ng. "Peptidyl-prolyl-cis/trans -isomerase activity may be necessary for memory formation." FEBS Letters 431, no. 3 (July 24, 1998): 386–90. http://dx.doi.org/10.1016/s0014-5793(98)00795-9.

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34

Takahashi, Nobuhiro, Toshiya Hayano, and Masanori Suzuki. "Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin." Nature 337, no. 6206 (February 1989): 473–75. http://dx.doi.org/10.1038/337473a0.

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35

OHASHI, Tsubasa, Sumito TESHIMA, Masafumi HIDAKA, and Takafumi UCHIDA. "Preparation of Protein Transduction Domain-Fused Peptidyl Prolyl cis/trans Isomerase Pin1." Bioscience, Biotechnology, and Biochemistry 74, no. 10 (October 23, 2010): 2067–70. http://dx.doi.org/10.1271/bbb.100372.

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36

COMPTON, Larry A., Janice M. DAVIS, J. Randy MACDONALD, and Hans Peter BACHINGER. "Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases." European Journal of Biochemistry 206, no. 3 (June 1992): 927–34. http://dx.doi.org/10.1111/j.1432-1033.1992.tb17002.x.

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37

Pissavin, Christine, and Nicole Hugouvieux-Cotte-Pattat. "Characterization of a periplasmic peptidyl-prolyl cis-trans isomerase in Erwinia chrysanthemi." FEMS Microbiology Letters 157, no. 1 (January 17, 2006): 59–65. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12753.x.

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38

Bissoli, Gaetano, Regina Niñoles, Sandra Fresquet, Samuela Palombieri, Eduardo Bueso, Lourdes Rubio, María J. García-Sánchez, José A. Fernández, José M. Mulet, and Ramón Serrano. "Peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis in Arabidopsis." Plant Journal 70, no. 4 (March 6, 2012): 704–16. http://dx.doi.org/10.1111/j.1365-313x.2012.04921.x.

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39

Weiwad, Matthias, Andreas Werner, Peter Rücknagel, Angelika Schierhorn, Gerd Küllertz, and Gunter Fischer. "Catalysis of Proline-directed Protein Phosphorylation by Peptidyl-prolyl cis/trans Isomerases." Journal of Molecular Biology 339, no. 3 (June 2004): 635–46. http://dx.doi.org/10.1016/j.jmb.2004.04.021.

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40

Nath, Pulak Ranjan, and Noah Isakov. "Insights into peptidyl-prolyl cis–trans isomerase structure and function in immunocytes." Immunology Letters 163, no. 1 (January 2015): 120–31. http://dx.doi.org/10.1016/j.imlet.2014.11.002.

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41

Tanaka, Yoshikazu, Arisa Amano, Masateru Morisaki, Yuka Sato, and Takashi Sasaki. "Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus." Antiviral Research 126 (February 2016): 1–7. http://dx.doi.org/10.1016/j.antiviral.2015.11.013.

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42

Lawen, Alfons. "Biosynthesis of cyclosporins and other natural peptidyl prolyl cis/trans isomerase inhibitors." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 10 (October 2015): 2111–20. http://dx.doi.org/10.1016/j.bbagen.2014.12.009.

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43

Gavini, Nara, Sudheer Tungtur, and Lakshmi Pulakat. "Peptidyl-Prolyl cis/trans Isomerase-Independent Functional NifH Mutant of Azotobacter vinelandii." Journal of Bacteriology 188, no. 16 (August 15, 2006): 6020–25. http://dx.doi.org/10.1128/jb.00379-06.

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ABSTRACT Peptidyl-prolyl cis/trans isomerases (PPIases) play a pivotal role in catalyzing the correct folding of many prokaryotic and eukaryotic proteins that are implicated in a variety of biological functions, ranging from cell cycle regulation to bacterial infection. The nif accessory protein NifM, which is essential for the biogenesis of a functional NifH component of nitrogenase, is a PPIase. To understand the nature of the molecular signature that defines the NifM dependence of NifH, we screened a library of nifH mutants in the nitrogen-fixing bacterium Azotobacter vinelandii for mutants that acquired NifM independence. Here, we report that NifH can acquire NifM independence when the conserved Pro258 located in the C-terminal region of NifH, which wraps around the other subunit in the NifH dimer, is replaced by serine.

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44

Stifani, Stefano. "The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer." Biomolecules 8, no. 4 (October 11, 2018): 112. http://dx.doi.org/10.3390/biom8040112.

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Peptidyl prolyl isomerases (PPIases) are broadly expressed enzymes that accelerate the cis-trans isomerization of proline peptide bonds. The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which isomerizes phosphorylated serine/threonine–proline bonds. By catalyzing this specific cis-trans isomerization, PIN1 can alter the structure of its target proteins and modulate their activities in a number of different ways. Many proteins are targets of proline-directed phosphorylation and thus PIN1-mediated isomerization of proline bonds represents an important step in the regulation of a variety of cellular mechanisms. Numerous other proteins in addition to PIN1 are endowed with PPIase activity. These include other members of the parvulin family to which PIN1 belongs, such as PIN4, as well as several cyclophilins and FK506-binding proteins. Unlike PIN1, however, these other PPIases do not isomerize phosphorylated serine/threonine–proline bonds and have different substrate specificities. PIN1 and other PPIases are overexpressed in many types of cancer and have been implicated in various oncogenic processes. This review will discuss studies providing evidence for multiple roles of PIN1 and other PPIases in glioblastoma and medulloblastoma, the most frequent adult and pediatric primary brain tumors.

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45

Jiang, Quan, Gang Wu, Lin Yang, Ya-Ping Lu, Xiu-Xiu Liu, Feng Han, Ya-Ping Deng, Xu-Chun Fu, Qi-Bing Liu, and Ying-Mei Lu. "Elucidation of the FKBP25-60S Ribosomal Protein L7a Stress Response Signaling During Ischemic Injury." Cellular Physiology and Biochemistry 47, no. 5 (2018): 2018–30. http://dx.doi.org/10.1159/000491470.

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Background/Aims: Peptidyl-prolyl cis-trans isomerase FKBP25 is a member of the FK506-binding proteins family which has peptidyl-prolyl cis/trans isomerase domain. The biological function and pathophysiologic role of FKBP25 remain elusive. Methods: The spatio-temporal changes in expression of endothelial FKBP25 upon oxygen-glucose deprivation (OGD) treatment were examined by Western blot and immunofluorescence. The immunoprecipitation and fluorescence resonance energy transfer (FRET) were used to address the interacting proteins with FKBP25. Results: In the present study, nuclear translocation of FKBP25 was observed following OGD in cultured endothelial cells. Intriguingly, FKBP25 nuclear translocation was further validated in peroxynitrite (ONOO-)-treated endothelial cells. Coimmunoprecipitation and FRET data indicated that FKBP25 translocated into the nucleus, in which it interacted with 60S ribosomal protein L7a, while overexpression FKBP25 protect endothelial cells against OGD injury. Conclusion: Our findings reveal that the nuclear import of FKBP25 and binding with 60S ribosomal protein L7a are protective stress responses to ischemia/nitrosaive stress injury.

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46

Rassow, J., K. Mohrs, S. Koidl, I. B. Barthelmess, N. Pfanner, and M. Tropschug. "Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60." Molecular and Cellular Biology 15, no. 5 (May 1995): 2654–62. http://dx.doi.org/10.1128/mcb.15.5.2654.

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Abstract:

We studied the role of mitochondrial cyclophilin 20 (CyP20), a peptidyl-prolyl cis-trans isomerase, in preprotein translocation across the mitochondrial membranes and protein folding inside the organelle. The inhibitory drug cyclosporin A did not impair membrane translocation of preproteins, but it delayed the folding of an imported protein in wild-type mitochondria. Similarly, Neurospora crassa mitochondria lacking CyP20 efficiently imported preproteins into the matrix, but folding of an imported protein was significantly delayed, indicating that CyP20 is involved in protein folding in the matrix. The slow folding in the mutant mitochondria was not inhibited by cyclosporin A. Folding intermediates of precursor molecules reversibly accumulated at the molecular chaperones Hsp70 and Hsp60 in the matrix. We conclude that CyP20 is a component of the mitochondrial protein folding machinery and that it cooperates with Hsp70 and Hsp60. It is speculated that peptidyl-prolyl cis-trans isomerases in other cellular compartments may similarly promote protein folding in cooperation with chaperone proteins.

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Daneri-Becerra, Cristina, Nadia R. Zgajnar, Cecilia M. Lotufo, Ana B. Ramos Hryb, Graciela Piwien-Pilipuk, and Mario D. Galigniana. "Regulation of FKBP51 and FKBP52 functions by post-translational modifications." Biochemical Society Transactions 47, no. 6 (November 22, 2019): 1815–31. http://dx.doi.org/10.1042/bst20190334.

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FKBP51 and FKBP52 are two iconic members of the family of peptidyl-prolyl-(cis/trans)-isomerases (EC: 5.2.1.8), which comprises proteins that catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds in unfolded and partially folded polypeptide chains and native state proteins. Originally, both proteins have been studied as molecular chaperones belonging to the steroid receptor heterocomplex, where they were first discovered. In addition to their expected role in receptor folding and chaperoning, FKBP51 and FKBP52 are also involved in many biological processes, such as signal transduction, transcriptional regulation, protein transport, cancer development, and cell differentiation, just to mention a few examples. Recent studies have revealed that both proteins are subject of post-translational modifications such as phosphorylation, SUMOlyation, and acetylation. In this work, we summarize recent advances in the study of these immunophilins portraying them as scaffolding proteins capable to organize protein heterocomplexes, describing some of their antagonistic properties in the physiology of the cell, and the putative regulation of their properties by those post-translational modifications.

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Wang, Yu, Chang Liu, Daiwen Yang, Hao Yu, and Yih-Cherng Liou. "Pin1At Encoding a Peptidyl-Prolyl cis/trans Isomerase Regulates Flowering Time in Arabidopsis." Molecular Cell 37, no. 1 (January 2010): 112–22. http://dx.doi.org/10.1016/j.molcel.2009.12.020.

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Harrison, Richard K., and Ross L. Stein. "Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion." Biochemistry 29, no. 7 (February 20, 1990): 1684–89. http://dx.doi.org/10.1021/bi00459a003.

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Henriksson, Lena M., Patrik Johansson, Torsten Unge, and Sherry L. Mowbray. "X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis." European Journal of Biochemistry 271, no. 20 (September 24, 2004): 4107–13. http://dx.doi.org/10.1111/j.1432-1033.2004.04348.x.

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