Zona pellucida-like domain explained

The zona pellucida-like domain (ZP domain / ZP-like domain / ZP module)[1] [2] is a large protein region of about 260 amino acids. It has been recognised in a variety of receptor-like eukaryotic glycoproteins.[1] All of these molecules are mosaic proteins with a large extracellular region composed of various domains, often followed by either a transmembrane region and a very short cytoplasmic region or by a GPI-anchor.[2]

Functional and crystallographic studies revealed that the "ZP domain" region common to all these proteins is a protein polymerization module that consists of two distinct but structurally related immunoglobulin-like domains, ZP-N and ZP-C.[3] [4] [5] [6] [7] [8] [9] [10] The ZP module is located in the C-terminal portion of the extracellular region and – with the exception of non-polymeric family member ENG[11] – contains 8 or 10 conserved Cys residues involved in disulfide bonds.[5] [6] [9]

The first 3D structure of a ZP module protein filament, native human uromodulin (UMOD), was determined by cryo-EM.[12] [13]

Additional copies of isolated ZP-N domains are found in the N-terminal region of egg coat protein subunits involved in fertilization in both vertebrates and invertebrates, such as human zona pellucida components ZP1, ZP2 and ZP4 and mollusk vitelline envelope receptor for egg lysin (VERL).[5] [14] [15]

Examples

Humans genes encoding proteins containing this domain include:

Notes and References

  1. Bork P, Sander C . A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor . FEBS Lett. . 300 . 3 . 237–40 . 1992 . 1313375 . 10.1016/0014-5793(92)80853-9. 38778076 . free .
  2. Jovine L, Darie CC, Litscher ES, Wassarman PM . Zona pellucida domain proteins . Annu. Rev. Biochem. . 74 . 83–114 . 2005 . 15952882 . 10.1146/annurev.biochem.74.082803.133039.
  3. Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM . The ZP domain is a conserved module for polymerization of extracellular proteins . Nat. Cell Biol. . 4 . 6 . 457–61 . 2002 . 12021773 . 10.1038/ncb802 . 11575790 .
  4. Jovine L, Qi H, Williams Z, Litscher ES, Wassarman PM . A duplicated motif controls assembly of zona pellucida domain proteins . Proc. Natl. Acad. Sci. U.S.A. . 101 . 16 . 5922–7 . 2004 . 15079052 . 10.1073/pnas.0401600101 . 395899 . 2004PNAS..101.5922J . free .
  5. Monné M, Han L, Schwend T, Burendahl S, Jovine L . Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats . Nature . 456 . 7222 . 653–7 . 2008 . 19052627 . 10.1038/nature07599 . 2008Natur.456..653M . 4430083 . 11563/8930 . free .
  6. Han L, Monné M, Okumura, H, Schwend, T, Cherry, AL, Flot, D, Matsuda, T, Jovine, L . Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3 . Cell . 143 . 3 . 404–15 . 2010 . 20970175 . 10.1016/j.cell.2010.09.041 . 18583237 . free . 11563/8931 . free .
  7. Lin SJ, Hu Y, Zhu J, Woodruff TK, Jardetzky TS . Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding . Proc Natl Acad Sci U S A . 108 . 13 . 5232–6 . 2011 . 21402931 . 10.1073/pnas.1010689108 . 3069177. 2011PNAS..108.5232L . free .
  8. Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA . Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3) . PLOS ONE . 8 . 6 . e67214 . 2013 . 23826237 . 10.1371/journal.pone.0067214 . 3695229. 2013PLoSO...867214D . free .
  9. Bokhove M, Nishimura K, Brunati M, Han L, de Sanctis D, Rampoldi L, Jovine L . A structured interdomain linker directs self-polymerization of human uromodulin . Proc. Natl. Acad. Sci. U.S.A. . 113 . 6 . 1552–1557 . 2016 . 26811476 . 10.1073/pnas.1519803113 . 4760807. 2016PNAS..113.1552B . free .
  10. Bokhove M, Jovine L . Structure of Zona Pellucida Module Proteins . Curr. Top. Dev. Biol. . Current Topics in Developmental Biology . 130 . 413–442 . 2018 . 29853186 . 10.1016/bs.ctdb.2018.02.007 . 9780128098028 .
  11. Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L . Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1 . Cell Reports . 19 . 9 . 1917–1928 . 2017 . 28564608 . 10.1016/j.celrep.2017.05.011 . 5464963.
  12. Stsiapanava A, Xu C, Brunati M, Zamora-Caballero S, Schaeffer C, Bokhove M, Han L, Hebert H, Carroni M, Yasumasu S, Rampoldi L, Wu B, Jovine L . Cryo-EM structure of native human uromodulin, a zona pellucida module polymer . EMBO J. . e106807 . 2020 . 39 . 24 . 33196145 . 7737619 . 10.15252/embj.2020106807 . free .
  13. Stsiapanava A, Xu C, Nishio S, Han L, Yamakawa N, Carroni M, Tunyasuvunakool K, Jumper J, de Sanctis D, Wu B, Jovine L . Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH . Nat. Struct. Mol. Biol. . 29 . 3 . 190–193 . 2022 . 35273390 . 10.1038/s41594-022-00729-3 . 8930769 . free .
  14. Callebaut I, Mornon JP, Monget P . Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins. . Bioinformatics . 23 . 1871–1874 . 17510169 . 10.1093/bioinformatics/btm265 . 2007. 15 . free .
  15. Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L . Structural Basis of Egg Coat-Sperm Recognition at Fertilization . Cell . 169 . 7 . 1315–1326 . 2017 . 28622512 . 10.1016/j.cell.2017.05.033 . 5480393.

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