Structure of Zona Pellucida Module Proteins

Current Topics in Developmental Biology
Marcel Bokhove, Luca Jovine

Abstract

The egg coat, an extracellular matrix made up of glycoprotein filaments, plays a key role in animal fertilization by acting as a gatekeeper for sperm. Egg coat components polymerize using a common zona pellucida (ZP) "domain" module that consists of two related immunoglobulin-like domains, called ZP-N and ZP-C. The ZP module has also been recognized in a large number of other secreted proteins with different biological functions, whose mutations are linked to severe human diseases. During the last decade, tremendous progress has been made toward understanding the atomic architecture of the ZP module and the structural basis of its polymerization. Moreover, sperm-binding regions at the N-terminus of mollusk and mammalian egg coat subunits were found to consist of domain repeats that also adopt a ZP-N fold. This discovery revealed an unexpected link between invertebrate and vertebrate fertilization and led to the first structure of an egg coat-sperm protein recognition complex. In this review we summarize these exciting findings, discuss their functional implications, and outline future challenges that must be addressed in order to develop a comprehensive view of this family of biomedically important extracellular molecules.

Citations

Jun 23, 2020·Annual Review of Biochemistry·Eveline S Litscher, Paul M Wassarman
Jan 27, 2019·Development·Isabel I C LowMaxwell G Heiman
Jul 14, 2019·Nature Communications·Kaoru NishimuraLuca Jovine
Oct 11, 2020·Journal of Developmental Biology·Jennifer D Cohen, Meera V Sundaram
Nov 4, 2020·PLoS Genetics·Jennifer D CohenMeera V Sundaram
Nov 17, 2020·The EMBO Journal·Alena StsiapanavaLuca Jovine
Feb 20, 2021·Journal of Assisted Reproduction and Genetics·Yiming SunCongjian Xu
Mar 6, 2021·Journal of Assisted Reproduction and Genetics·Jing WangXiang Ma

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