Characterization of gametogenetin 1 (GGN1) and its potential role in male fertility through the interaction with the ion channel regulator, cysteine-rich secretory protein 2 (CRISP2) in the sperm tail
| Autor: | Donna Jo Merriner, Deborah M. Bianco, Moira K O'Bryan, Stephanie Jay Smith, Gerard M. Gibbs, Jennifer D Ly-Huynh, Birunthi Niranjan, Amy Herlihy, Duangporn Jamsai |
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| Rok vydání: | 2008 |
| Předmět: |
Male
Embryology Amino Acid Motifs Blotting Western Molecular Sequence Data Plasma protein binding Andrology Mice Endocrinology Cysteine-rich secretory protein Spermatocytes MAP3K11 Two-Hybrid System Techniques Testis Animals Amino Acid Sequence Cloning Molecular Spermatogenesis Glycoproteins Messenger RNA Base Sequence biology MAP kinase kinase kinase Chemistry cDNA library Membrane Proteins Obstetrics and Gynecology Cell Biology Blotting Northern Immunohistochemistry Spermatids Sperm Cell biology Testicular Hormones Secretory protein Reproductive Medicine Sperm Tail Sperm Motility biology.protein Genetic Engineering Acrosome Cell Adhesion Molecules Protein Binding |
| Zdroj: | REPRODUCTION. 135:751-759 |
| ISSN: | 1741-7899 1470-1626 |
| DOI: | 10.1530/rep-07-0485 |
| Popis: | Cysteine-rich secretory protein 2 (CRISP2) is a testis-enriched protein localized to the sperm acrosome and tail. CRISP2 has been proposed to play a critical role in spermatogenesis and male fertility, although the precise function(s) of CRISP2 remains to be determined. Recent data have shown that the CRISP domain of the mouse CRISP2 has the ability to regulate Ca2+flow through ryanodine receptors (RyR) and to bind to MAP kinase kinase kinase 11 (MAP3K11). To further define the biochemical pathways within which CRISP2 is involved, we screened an adult mouse testis cDNA library using a yeast two-hybrid assay to identify CRISP2 interacting partners. One of the most frequently identified CRISP2-binding proteins was gametogenetin 1 (GGN1). Interactions occur between the ion channel regulatory region within the CRISP2 CRISP domain and the carboxyl-most 158 amino acids of GGN1. CRISP2 does not bind to the GGN2 or GGN3 isoforms. Furthermore, we showed thatGgn1is a testis-enriched mRNA and the protein first appeared in late pachytene spermatocytes and was up-regulated in round spermatids before being incorporated into the principal piece of the sperm tail where it co-localized with CRISP2. These data along with data on RyR and MAP3K11 binding define the CRISP2 CRISP domain as a protein interaction motif and suggest a role for the GGN1–CRISP2 complex in sperm tail development and/or motility. |
| Databáze: | OpenAIRE |
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