Biol Reprod Keystone Symposia Conference on Frontiers in Reproductive Biology & Regulation of Fertility.
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BOR - Papers in Press, published online ahead of print May 7, 2008.
Biol Reprod 2008, 10.1095/biolreprod.108.069328
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BIOLOGY OF REPRODUCTION 79, 337–347 (2008)
DOI: 10.1095/biolreprod.108.069328
© 2008 by the Society for the Study of Reproduction, Inc.

research-article

Phosphorylation-Dependent Interaction of Tyrosine 3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein (YWHA) with PADI6 Following Oocyte Maturation in Mice1

Alan J. Snow 3, Pawan Puri 3, Amparo Acker-Palmer 4, Tewis Bouwmeester 5, Srinivasan Vijayaraghavan 3, and Douglas Kline 2 3

Department of Biological Sciences,3 Kent State University, Kent, Ohio 44242 Cluster of Excellence Macromolecular Complexes,4 Institute of Cell Biology and Neuroscience, Goethe University Frankfurt, D-60438 Frankfurt am Main, Germany Cellzome AG,5 69117 Heidelberg, Germany

ABSTRACT

Proteins in the tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein family (YWHA; also known as 14-3-3) are involved in the regulation of many intracellular processes. We have examined the interaction of YWHA with peptidylarginine deiminase type VI (PADI6), an abundant protein in mammalian oocytes, eggs, and early embryos. Peptidylarginine deiminases catalyze the posttranslational modification of peptidylarginine to citrulline. PADI6 is associated with oocyte cytoplasmic sheets, and PADI6-deficient mice are infertile because of disruption of development beyond the two-cell stage. We found that PADI6 undergoes a dramatic developmental change in phosphorylation during oocyte maturation. This change in phosphorylation is linked to an interaction of PADI6 with YWHA in the mature egg. Recombinant glutathione S-transferase YWHA pull-down experiments and transgenic tandem affinity purification with liquid chromatography-mass spectrometry demonstrate a binding interaction between YWHA and PADI6 in mature eggs. YWHA proteins modulate or complement intracellular events involving phosphorylation-dependent switching or protein modification. These results indicate that phosphorylation and/or YWHA binding may serve as a means of intracellular PADI6 regulation.

egg, gamete biology, gametogenesis, mouse, oocyte, oocyte development, oocyte maturation, ovum, PADI6, PAD6, peptidylarginine deiminase, phosphorylation, YWHA, 14-3-3

FOOTNOTES

1Supported by National Institutes of Health grant HD38520 to S.V.

Correspondence: 2D. Kline, Department of Biological Sciences, Kent State University, Kent, OH 44242. FAX: 330 672 3713; e-mail: dline{at}kent.edu






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Copyright © 2008 by the Society for the Study of Reproduction.