Biology:Parvulin 14

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Short description: Member of the parvulin family

Par14 (eukaryotic homolog of parvulin, EHPF) is a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases (PPIases) in humans, which possesses prolyl isomerase activity.[1]

History

In 1999, Par14 was identified by two groups independently.[2][3] After the discovery of human Pin1 in 1996,[4] Par14 turned out to be the second member of the human parvulin family. In contrast to Pin1, Par14 exhibits minor catalytic activity, shows no preference for phosphorylated substrates[2] and fails to rescue the loss of the Pin1-related parvulin Ess1 in yeast.[5] Par14 orthologs are found in many unicellular eukaryotes and all multicellular organisms. In 2006, a Par14 isoform, denoted Par17, was described, which carries an N-terminal extension of 25 residues and is exclusively expressed in hominids.[6]

Expression and localization

Par14 originates from transcription of the PIN4 gene on chromosome Xq13.1. The promotor region is TATA-less and located within a CpG island.[6] The protein is primarily active within the nucleus/nucleolus of the cell, but also found within the cytoplasm.[3][4][5][6][7]

Biological function

Cytoplasm: Par14 interacts with the insulin receptor substrate (IRS-1) and enhances insulin-induced tyrosine-phosphorylation of IRS-1.[8] During mitosis Par14 associates to the spindle apparatus.[7] In vitro experiments demonstrated that Par14 may be involved in filament polymerization.[9][10]

Nucleus/Nucleolus: Phosphorylation of Ser19 by casein kinase 2 translocates Par14 into the cellular nucleus.[11] After dephosphorylation the protein associates to chromatin,[12] with the N-terminus mainly responsible for high-affinity DNA binding.[13] Par14 is found in pre-ribosomal ribonuclear protein complexes, where it acts as an rRNA processing factor.[7][14] Photoaffinity labeling and Liquid chromatography–mass spectrometry analysis reveal the enzyme to be associated with proteins functioning in DNA replication, DNA repair and/or chromatin remodeling.[10] Par14 requires phosphorylation of Ser7 and Ser9 by protein kinase B (Akt) (or protein kinase C) for nuclear export. This export is probably maintained by 14-3-3 protein in a Crm1 dependent way.[15]

Structure

Par14’s catalytic domain exhibits the typical parvulin fold (order of secondary structure elements β1-α1-α2-h-β2-α3-β3-β4; α = α-helix, β = β-strand, h = helical turn) found in all members of this family, so far.[16] Its three-dimensional structure PDB-ID: 3UI4 PDB-ID: 1EQ3 is characterized by a ‘gripping hand’ topology with the central β-sheet core (consisting of four antiparallel strands) opposing α-helix 3. The catalytic center resides on the concave side of the β-sheet.[16][17] An N-terminal IDR-like stretch composed of mainly small or basic residues precedes this domain. The IDR element is prone to post-translational modifications.

Disease related function/clinical aspects

Par14 is involved in the upregulation of hepatitis B virus replication.[18] Expression of Par14 correlates to primary biliary cirrhosis, an autoimmune chronic cholestatic liver disease.[19] K-RAS exosomes of collateral cancer cells were found to carry Par14.[20]

References

  1. ↑ Matena, Anja; Rehic, Edisa; Hönig, Dana; Kamba, Bianca; Bayer, Peter (2018). "Structure and function of the human parvulins Pin1 and Par14/17". Biological Chemistry 399 (2): 101–125. doi:10.1515/hsz-2017-0137. PMID 29040060. 
  2. ↑ 2.0 2.1 Uchida, Takafumi; Fujimori, Fumihiro; Tradler, Thomas; Fischer, Gunter; Rahfeld, Jens-U (1999). "Identification and characterization of a 14 k Da human protein as a novel parvulin-like peptidyl prolyl cis /Trans isomerase". FEBS Letters 446 (2–3): 278–282. doi:10.1016/s0014-5793(99)00239-2. PMID 10100858. 
  3. ↑ 3.0 3.1 Thorpe, Julian R.; Rulten, Stuart L.; Kay, John E. (1999). "Binding of a Putative and a Known Chaperone Protein Revealed by Immunogold Labeling Transmission Electron Microscopy: A Suggested Use of Chaperones as Probes for the Distribution of Their Target Proteins". Journal of Histochemistry & Cytochemistry 47 (12): 1633–1640. doi:10.1177/002215549904701215. PMID 10567447. 
  4. ↑ 4.0 4.1 Ping Lu, Kun; Hanes, Steven D.; Hunter, Tony (1996). "A human peptidyl–prolyl isomerase essential for regulation of mitosis". Nature 380 (6574): 544–547. doi:10.1038/380544a0. PMID 8606777. Bibcode: 1996Natur.380..544P. 
  5. ↑ 5.0 5.1 Metzner, Martin; Stoller, Gerlind; Rücknagel, Karl P.; Lu, Kun Ping; Fischer, Gunter; Luckner, Martin; Küllertz, Gerhard (2001). "Functional Replacement of the Essential ESS1 in Yeast by the Plant ParvulinDlPar13". Journal of Biological Chemistry 276 (17): 13524–13529. doi:10.1074/jbc.M007005200. PMID 11118437. 
  6. ↑ 6.0 6.1 6.2 Mueller, Jonathan; Kessler, Daniel; Neumann, Daniel; Stratmann, Tina; Papatheodorou, Panagiotis; Hartmann-Fatu, Cristina; Bayer, Peter (2006). "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation". BMC Molecular Biology 7: 9. doi:10.1186/1471-2199-7-9. PMID 16522211. 
  7. ↑ 7.0 7.1 7.2 Fujiyama-Nakamura, Sally; Yoshikawa, Harunori; Homma, Keiichi; Hayano, Toshiya; Tsujimura-Takahashi, Teruko; Izumikawa, Keiichi; Ishikawa, Hideaki; Miyazawa, Naoki et al. (2009). "Parvulin (Par14), a Peptidyl-Prolylcis-trans Isomerase, is a Novel rRNA Processing Factor That Evolved in the Metazoan Lineage". Molecular & Cellular Proteomics 8 (7): 1552–1565. doi:10.1074/mcp.M900147-MCP200. PMID 19369196. 
  8. ↑ Zhang, Jun; Nakatsu, Yusuke; Shinjo, Takanori; Guo, Ying; Sakoda, Hideyuki; Yamamotoya, Takeshi; Otani, Yuichiro; Okubo, Hirofumi et al. (2013). "Par14 Protein Associates with Insulin Receptor Substrate 1 (IRS-1), Thereby Enhancing Insulin-induced IRS-1 Phosphorylation and Metabolic Actions". Journal of Biological Chemistry 288 (28): 20692–20701. doi:10.1074/jbc.M113.485730. PMID 23720771. 
  9. ↑ Thiele, Alexandra; Krentzlin, Karolin; Erdmann, Frank; Rauh, David; Hause, Gerd; Zerweck, Johannes; Kilka, Susann; Pösel, Stephanie et al. (2011). "Parvulin 17 Promotes Microtubule Assembly by Its Peptidyl-Prolyl Cis/Trans Isomerase Activity". Journal of Molecular Biology 411 (4): 896–909. doi:10.1016/j.jmb.2011.06.040. PMID 21756916. 
  10. ↑ 10.0 10.1 Goehring, Anna; Michin, Irina; Gerdes, Tina; Schulze, Nina; Blueggel, Mike; Rehic, Edisa; Kaschani, Farnusch; Kaiser, Markus et al. (2020). "Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization". Biological Chemistry 401 (8): 955–968. doi:10.1515/hsz-2019-0423. PMID 32142471. 
  11. ↑ Reimer, Tatiana; Weiwad, Matthias; Schierhorn, Angelika; Ruecknagel, Peter-Karl; Rahfeld, Jens-Ulrich; Bayer, Peter; Fischer, Gunter (2003). "Phosphorylation of the N-terminal Domain Regulates Subcellular Localization and DNA Binding Properties of the Peptidyl-prolyl cis/Trans Isomerase hPar14". Journal of Molecular Biology 330 (5): 955–966. doi:10.1016/s0022-2836(03)00713-7. PMID 12860119. 
  12. ↑ Saningong, Akuma D.; Bayer, Peter (2015). "Human DNA-binding peptidyl-prolyl cis/Trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo". BMC Biochemistry 16: 4. doi:10.1186/s12858-015-0033-x. PMID 25645591. 
  13. ↑ Surmacz, Tatiana Anna; Bayer, Elena; Rahfeld, Jens-Ulrich; Fischer, Gunter; Bayer, Peter (2002). "The N-terminal Basic Domain of Human Parvulin hPar14 is Responsible for the Entry to the Nucleus and High-affinity DNA-binding". Journal of Molecular Biology 321 (2): 235–247. doi:10.1016/s0022-2836(02)00615-0. PMID 12144781. 
  14. ↑ Fujiyama, Sally; Yanagida, Mitsuaki; Hayano, Toshiya; Miura, Yutaka; Isobe, Toshiaki; Takahashi, Nobuhiro; Uchida, T.; Takahashi, N. (2002). "Isolation and Proteomic Characterization of Human Parvulin-associating Preribosomal Ribonucleoprotein Complexes". Journal of Biological Chemistry 277 (26): 23773–23780. doi:10.1074/jbc.M201181200. PMID 11960984. 
  15. ↑ Reimer T (2003), Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14. PhD thesis, https://sundoc.bibliothek.uni-halle.de/diss-online/03/03H115/of_index.htm 
  16. ↑ 16.0 16.1 Sekerina, Elena; Rahfeld, Jens Ulrich; Müller, Jonathan; Fanghänel, Jörg; Rascher, Christine; Fischer, Gunter; Bayer, Peter (2000). "NMR solution structure of h Par14 reveals similarity to the peptidyl prolyl cis/Trans isomerase domain of the mitotic regulator h Pin1 but indicates a different functionality of the protein 1 1Edited by A. Fersht". Journal of Molecular Biology 301 (4): 1003–1017. doi:10.1006/jmbi.2000.4013. PMID 10966801. 
  17. ↑ Terada, Tohru; Shirouzu, Mikako; Fukumori, Yasuhiro; Fujimori, Fumihiro; Ito, Yutaka; Kigawa, Takanori; Yokoyama, Shigeyuki; Uchida, Takafumi (2001). "Solution structure of the human parvulin-like peptidyl prolyl cis/Trans isomerase, hPar14". Journal of Molecular Biology 305 (4): 917–926. doi:10.1006/jmbi.2000.4293. PMID 11162102. 
  18. ↑ Saeed, Umar; Kim, Jumi; Piracha, Zahra Zahid; Kwon, Hyeonjoong; Jung, Jaesung; Chwae, Yong-Joon; Park, Sun; Shin, Ho-Joon et al. (2018). "Parvulin 14 and Parvulin 17 Bind to HBX and cccDNA and Upregulate Hepatitis B Virus Replication from cccDNA to Virion in an HBX-Dependent Manner". Journal of Virology 93 (6). doi:10.1128/JVI.01840-18. PMID 30567987. 
  19. ↑ Mitchell, Michelle M.; Lleo, Ana; Zammataro, Luca; Mayo, Marlyn J.; Invernizzi, Pietro; Bach, Nancy; Shimoda, Shinji; Gordon, Stuart et al. (2011). "Epigenetic investigation of variably X chromosome inactivated genes in monozygotic female twins discordant for primary biliary cirrhosis". Epigenetics 6 (1): 95–102. doi:10.4161/epi.6.1.13405. PMID 20864813. 
  20. ↑ Demory Beckler, Michelle; Higginbotham, James N.; Franklin, Jeffrey L.; Ham, Amy-Joan; Halvey, Patrick J.; Imasuen, Imade E.; Whitwell, Corbin; Li, Ming et al. (2013). "Proteomic Analysis of Exosomes from Mutant KRAS Colon Cancer Cells Identifies Intercellular Transfer of Mutant KRAS". Molecular & Cellular Proteomics 12 (2): 343–355. doi:10.1074/mcp.M112.022806. PMID 23161513. 



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