The ZP domain is a conserved module for polymerization of extracelluar proteins

Luca Jovine, Huayu Qi, Zev Williams, Eveline Litscher, Paul M. Wassarman

Research output: Contribution to journalArticle

225 Citations (Scopus)

Abstract

Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), α- and β-tectorins, transforming growth factor (TGF)-β receptor III and endoglin, DMBT-1 (deletd in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2). Here, we report that the ZP domain of ZP2, ZP3 and THP is responsible for polymerization of these proteins into filaments of similar supramolecular structure. Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors. Our results demonstrate that the C-terminal transmembrane domain and short cytoplasmic tail of ZP2 and ZP3 are not required for secretion, but are essential for assembly. Finally, we suggest a molecular basis for dominant human hearing disorders caused by point mutations within the ZP domain of α-tectorin.

Original languageEnglish (US)
Pages (from-to)457-461
Number of pages5
JournalNature Cell Biology
Volume4
Issue number6
DOIs
StatePublished - 2002
Externally publishedYes

Fingerprint

Zona Pellucida
Uromodulin
Polymerization
Proteins
Hearing Disorders
Egg Proteins
Glycosylphosphatidylinositols
Mechanoreceptors
Growth Factor Receptors
Capsid Proteins
Transforming Growth Factors
Point Mutation
Brain Neoplasms
Tail

ASJC Scopus subject areas

  • Cell Biology

Cite this

Jovine, L., Qi, H., Williams, Z., Litscher, E., & Wassarman, P. M. (2002). The ZP domain is a conserved module for polymerization of extracelluar proteins. Nature Cell Biology, 4(6), 457-461. https://doi.org/10.1038/ncb802

The ZP domain is a conserved module for polymerization of extracelluar proteins. / Jovine, Luca; Qi, Huayu; Williams, Zev; Litscher, Eveline; Wassarman, Paul M.

In: Nature Cell Biology, Vol. 4, No. 6, 2002, p. 457-461.

Research output: Contribution to journalArticle

Jovine, L, Qi, H, Williams, Z, Litscher, E & Wassarman, PM 2002, 'The ZP domain is a conserved module for polymerization of extracelluar proteins', Nature Cell Biology, vol. 4, no. 6, pp. 457-461. https://doi.org/10.1038/ncb802
Jovine, Luca ; Qi, Huayu ; Williams, Zev ; Litscher, Eveline ; Wassarman, Paul M. / The ZP domain is a conserved module for polymerization of extracelluar proteins. In: Nature Cell Biology. 2002 ; Vol. 4, No. 6. pp. 457-461.
@article{c96d61c2066a445b8113a5a6d27029d4,
title = "The ZP domain is a conserved module for polymerization of extracelluar proteins",
abstract = "Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), α- and β-tectorins, transforming growth factor (TGF)-β receptor III and endoglin, DMBT-1 (deletd in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2). Here, we report that the ZP domain of ZP2, ZP3 and THP is responsible for polymerization of these proteins into filaments of similar supramolecular structure. Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors. Our results demonstrate that the C-terminal transmembrane domain and short cytoplasmic tail of ZP2 and ZP3 are not required for secretion, but are essential for assembly. Finally, we suggest a molecular basis for dominant human hearing disorders caused by point mutations within the ZP domain of α-tectorin.",
author = "Luca Jovine and Huayu Qi and Zev Williams and Eveline Litscher and Wassarman, {Paul M.}",
year = "2002",
doi = "10.1038/ncb802",
language = "English (US)",
volume = "4",
pages = "457--461",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "6",

}

TY - JOUR

T1 - The ZP domain is a conserved module for polymerization of extracelluar proteins

AU - Jovine, Luca

AU - Qi, Huayu

AU - Williams, Zev

AU - Litscher, Eveline

AU - Wassarman, Paul M.

PY - 2002

Y1 - 2002

N2 - Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), α- and β-tectorins, transforming growth factor (TGF)-β receptor III and endoglin, DMBT-1 (deletd in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2). Here, we report that the ZP domain of ZP2, ZP3 and THP is responsible for polymerization of these proteins into filaments of similar supramolecular structure. Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors. Our results demonstrate that the C-terminal transmembrane domain and short cytoplasmic tail of ZP2 and ZP3 are not required for secretion, but are essential for assembly. Finally, we suggest a molecular basis for dominant human hearing disorders caused by point mutations within the ZP domain of α-tectorin.

AB - Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), α- and β-tectorins, transforming growth factor (TGF)-β receptor III and endoglin, DMBT-1 (deletd in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2). Here, we report that the ZP domain of ZP2, ZP3 and THP is responsible for polymerization of these proteins into filaments of similar supramolecular structure. Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors. Our results demonstrate that the C-terminal transmembrane domain and short cytoplasmic tail of ZP2 and ZP3 are not required for secretion, but are essential for assembly. Finally, we suggest a molecular basis for dominant human hearing disorders caused by point mutations within the ZP domain of α-tectorin.

UR - http://www.scopus.com/inward/record.url?scp=0036307181&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036307181&partnerID=8YFLogxK

U2 - 10.1038/ncb802

DO - 10.1038/ncb802

M3 - Article

VL - 4

SP - 457

EP - 461

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 6

ER -