The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells.
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 the development of the human germ cells.
Ginter-Matuszewska
B
B
Institute of Human Genetics Polish Academy of Sciences, Poznan, Poland.
Spik
A
A
Rembiszewska
A
A
Koyias
C
C
Kupryjanczyk
J
J
Jaruzelska
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D005854:Germ Cells / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D047468:Immunoprecipitation; D066298:In Vitro Techniques; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011485:Protein Binding; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012671:Seminiferous Tubules / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D020798:Two-Hybrid System Techniques; D033921:Vesicular Transport Proteins / Q000737:chemistry / Q000378:metabolism*
C515170:NANOS1 protein, human; C471243:PUM2 protein, human; D016601:RNA-Binding Proteins; C118519:SNAPIN protein, human; C498451:Snapin protein, mouse; D033921:Vesicular Transport Proteins