PUBLICATION

hnRNP I is required to generate the Ca2+ signal that causes egg activation in zebrafish

Authors
Mei, W., Lee, K.W., Marlow, F.L., Miller, A.L., and Mullins, M.C.
ID
ZDB-PUB-090814-10
Date
2009
Source
Development (Cambridge, England)   136(17): 3007-3017 (Journal)
Registered Authors
Lee, Karen W., Marlow, Florence, Mei, Wenyan, Miller, Andrew L., Mullins, Mary C.
Keywords
hnRNP I, brom bones, IP3, Ca2+, Egg activation, Zebrafish, Cortical granule exocytosis, Maternal effect
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Calcium/metabolism*
  • Calcium Signaling/physiology*
  • Endoplasmic Reticulum/metabolism
  • Female
  • Heterogeneous-Nuclear Ribonucleoproteins/genetics
  • Heterogeneous-Nuclear Ribonucleoproteins/metabolism*
  • Humans
  • Inositol 1,4,5-Trisphosphate/metabolism
  • Microtubules/metabolism
  • Molecular Sequence Data
  • Oocytes/cytology
  • Oocytes/physiology*
  • Phenotype
  • Sequence Alignment
  • Zebrafish*/embryology
  • Zebrafish*/physiology
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed
19666827 Full text @ Development
Abstract
Egg activation is an important cellular event required to prevent polyspermy and initiate development of the zygote. Egg activation in all animals examined is elicited by a rise in free Ca(2+) in the egg cytosol at fertilization. This Ca(2+) rise is crucial for all subsequent egg activation steps, such as cortical granule exocytosis, which modifies the vitelline membrane to prevent polyspermy. The cytosolic Ca(2+) rise is primarily initiated by inositol 1,4,5-trisphosphate (IP(3))-mediated Ca(2+) release from the endoplasmic reticulum. The genes involved in regulating the IP(3)-mediated Ca(2+) release during egg activation remain largely unknown. Here we report on a zebrafish maternal-effect mutant, brom bones, which is defective in the cytosolic Ca(2+) rise and subsequent egg activation events, including cortical granule exocytosis and cytoplasmic segregation. We show that the egg activation defects in brom bones can be rescued by providing Ca(2+) or the Ca(2+)-release messenger IP(3), suggesting that brom bones is a regulator of IP(3)-mediated Ca(2+) release at fertilization. Interestingly, brom bones mutant embryos also display defects in dorsoventral axis formation accompanied by a disorganized cortical microtubule network, which is known to be crucial for dorsal axis formation. We provide evidence that the impaired microtubule organization is associated with non-exocytosed cortical granules from the earlier egg activation defect. Positional cloning of the brom bones gene reveals that a premature stop codon in the gene encoding hnRNP I (referred to here as hnrnp I) underlies the abnormalities. Our studies therefore reveal an important new role of hnrnp I in regulating the fundamental process of IP(3)-mediated Ca(2+) release at egg activation.
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Human Disease / Model
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Mapping