| Literature DB >> 19879147 |
Jean M Parry1, Nathalie V Velarde, Ariel J Lefkovith, Matthew H Zegarek, Julie S Hang, Jonathan Ohm, Richard Klancer, Rika Maruyama, Marina K Druzhinina, Barth D Grant, Fabio Piano, Andrew Singson.
Abstract
The molecular underpinnings of the oocyte-to-embryo transition are poorly understood. Here we show that two protein tyrosine phosphatase-like (PTPL) family proteins, EGG-4 and EGG-5, are required for key events of the oocyte-to-embryo transition in Caenorhabditis elegans. The predicted EGG-4 and EGG-5 amino acid sequences are 99% identical and their functions are redundant. In embryos lacking EGG-4 and EGG-5, we observe defects in meiosis, polar body formation, the block to polyspermy, F-actin dynamics, and eggshell deposition. During oogenesis, EGG-4 and EGG-5 assemble at the oocyte cortex with the previously identified regulators or effectors of the oocyte-to-embryo transition EGG-3, CHS-1, and MBK-2 [1, 2]. All of these molecules share a complex interdependence with regards to their dynamics and subcellular localization. Shortly after fertilization, EGG-4 and EGG-5 are required to properly coordinate a redistribution of CHS-1 and EGG-3 away from the cortex during meiotic anaphase I. Therefore, EGG-4 and EGG-5 are not only required for critical events of the oocyte-to-embryo transition but also link the dynamics of the regulatory machinery with the advancing cell cycle.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19879147 PMCID: PMC2783797 DOI: 10.1016/j.cub.2009.09.015
Source DB: PubMed Journal: Curr Biol ISSN: 0960-9822 Impact factor: 10.834