Mol. Hum. Reprod. Advance Access published online on January 23, 2009
Molecular Human Reproduction, doi:10.1093/molehr/gap004
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The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells
czyk21 Institute of Human Genetics Polish Academy of Sciences, 60-479 Poznan, Poland 2Department of Molecular Pathology, Center of Oncology, 02-781Warsaw, Poland
3 To whom correspondence should be addressed: Jadwiga Jaruzelska, Ph.D. Institute of Human Genetics Polish Academy of Sciences Strzeszynska 32, 60-479 Poznan, Poland Tel: 4861 657 9208 Fax: 4861 823 3235 jaruzjad{at}man.poznan.pl
It has been reported that a highly conserved human protein PUMILIO2 forms a complex with NANOS1 in human male germ cells, as does the Drosophila ancestor Pumilio, which binds Nanos to regulate translation of specific mRNAs.
Here, we found that PUMILIO2 interacts also with SNAPIN, a modulator of SNARE complex assembly, which is involved in vesicle trafficking. We demonstrated that SNAPIN interacts additionally with NANOS1 protein. This is the first report demonstrating that the N-terminal region of NANOS1 is necessary for protein binding. In human testis, SNAPIN co-localizes with PUMILIO2 and NANOS1 in prenatal and also in spermatogenic germ cells of the adult. We describe for the first time the expression of SNAPIN in germ cells which raises possibility that SNAPIN plays an extra role in mammals which is germ cell specific. The presence of a coiled-coil domain responsible for protein-protein interaction could enable SNAPIN to be an adaptor of PUMILIO2 and NANOS1, binding other factors to regulate translation in development of the human germ cells.
Key Words: germ cells/NANOS1/PUMILIO2/SNAPIN/spermatogenesis
Submitted on February 20, 2008; resubmitted on January 7, 2009; accepted on January 15, 2009.