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Parvulin 14

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Par14 (eukaryotic homolog of parvulin, EHPF) is a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases (PPIases) in humans, which posseses 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.

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 A, Rehic E, Hönig D, Kamba B, Bayer P. (2018) Structure and function of the human parvulins Pin1 and Par14/17. Biol Chem 399, 101-125. doi:10.1515/hsz-2017-0137
  2. ^ a b Uchida T, Fujimori F, Tradler T, Fischer G and Rahfeld JU (1999). Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett 446, 278–282. DOI: 10.1016/s0014-5793(99)00239-2
  3. ^ a b Thorpe JR, Rulten SL and Kay JE (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. J Histochem Cytochem 47, 1633–1640. DOI: 10.1177/002215549904701215
  4. ^ a b Lu KP, Hanes SD and Hunter T (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544–547. DOI: 10.1038/380544a0
  5. ^ a b Metzner M, Stoller G, Rucknagel KP, Lu KP, Fischer G, Luckner M, Küllertz G (2001). Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem 276, 13524–13529. DOI: 10.1074/jbc.M007005200
  6. ^ a b c Mueller JW, Kessler D, Neumann D, Stratmann T, Papatheodorou P, Hartmann-Fatu C and Bayer P (2006) Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation. BMC Mol Biol 7:9. doi:10.1186/1471-2199-7-9
  7. ^ a b c Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. (2009). Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics 8, 1552–1565. DOI: 10.1074/mcp.M900147-MCP200
  8. ^ Zhang J, Nakatsu Y, Shinjo T, Guo Y, Sakoda H, Yamamotoya T, Otani Y, Okubo H, Kushiyama A, Fujishiro M, Fukushima T, Tsuchiya Y, Kamata H, Iwashita M, Nishimura F, Katagiri H, Takahashi S, Kurihara H, Uchida T, Asano T (2013). Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions. J Biol Chem 288, 20692–20701. doi: 10.1074/jbc.M113.485730
  9. ^ Thiele A, Krentzlin K, Erdmann F, Rauh D, Hause G, Zerweck J, Kilka S, Pösel S, Fischer G, Schutkowski M, Weiwad M (2011) Parvulin 17 promotes microtubule assembly by its peptidyl-prolyl cis/trans isomerase activity. J Mol Biol 411, 896–909. doi: 10.1016/j.jmb.2011.06.040
  10. ^ a b Goehring A, Michin I, Gerdes T, Schulze N, Blueggel M, Rehic E, Kaschani F, Kaiser M, Bayer P (2020) Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization. Biol Chem 401, 955-968. doi: 10.1515/hsz-2019-0423
  11. ^ Reimer T, Weiwad M, Schierhorn A, Ruecknagel PK, Rahfeld JU, Bayer P, Fischer G (2003) Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14. J Mol Biol 330, 955-966. DOI: 10.1016/s0022-2836(03)00713-7
  12. ^ Saningong AD and Bayer P (2015). Human DNA-binding peptidyl-prolyl cis/trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo. BMC Biochem 16, 4. doi: 10.1186/s12858-015-0033-x
  13. ^ Surmacz TA, Bayer E, Rahfeld JU, Fischer G, Bayer P (2002) The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding. J Mol Biol 321, 235-247. DOI: 10.1016/s0022-2836(02)00615-0
  14. ^ Fujiyama S, Yanagida M, Hayano T, Miura Y, Isobe T, Fujimori F, Uchida T, Takahashi N (2002). Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes. J Biol Chgem 277, 23773–23780. DOI: 10.1074/jbc.M201181200
  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. ^ a b Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P (2000). NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein. J Mol Biol 301, 1003–1017. DOI: 10.1006/jmbi.2000.4013.
  17. ^ Terada T, Shirouzu M, Fukumori Y, Fujimori F, Ito Y, Kigawa T, Yokoyama S, Uchida T (2001) Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14. J Mol Biol 305, 917–926. Doi: 10.1006/jmbi.2000.4293
  18. ^ Saeed U, Kim J, Piracha ZZ, Kwon H, Jung J, Chwae YJ, Park S, Shin HJ, Kim K (2019) 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. J Virol 93, e01840-18. doi: 10.1128/JVI.01840-18
  19. ^ Mitchell MM, Lleo A, Zammataro L, Mayo MJ, Invernizzi P, Bach N, Shimoda S, Gordon S, Podda M, Gershwin ME, Selmi C, LaSalle JM (2011). Epigenetic investigation of variably X chromosome inactivated genes in monozygotic female twins discordant for primary biliary cirrhosis. Epigenetics 6, 95–102. DOI: 10.4161/epi.6.1.13405
  20. ^ Demory Beckler M, Higginbotham JN, Franklin JL, Ham AJ, Halvey PJ, Imasuen IE, Whitwell C, Li M, Liebler DC, Coffey RJ (2013). Proteomic analysis of exosomes from mutant KRAS colon cancer cells identifies intercellular transfer of mutant KRAS. Mol. Cell. Proteomics 12, 343–355. DOI: 10.1074/mcp.M112.022806

Category:EC 5.2.1

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