Vps20-associated 1 (Vta1) positively regulates Vacuolar protein sorting 4 (Vps4) to disassemble endosomal sorting complex required for transport III (ESCRT-III) for repeated uses in multivesicular body (MVB) pathway, virus budding and other processes. Currently, these proteins have mainly been studied in yeast and mammalian cells, while identities of them in insects remain largely unknown. We previously identified BmVps4, a Vps4 homologue from Bombyx mori. Here, we report the identification of a homologue for Vta1, designated as BmVta1. The BmVta1 cDNA contains an open reading frame of 933 bp and encodes a protein of 311 amino acid residues. We cloned BmVta1, expressed it in Escherichia coli, and prepared mouse polyclonal antibodies. Like BmVps4, BmVta1 is well conserved as shown by sequence analysis. Both proteins are localized in cytoplasm as revealed by subcellular location analysis. Interestingly, as revealed by semi-quantitative reverse transcription polymerase chain reaction (sqRT-PCR), transcriptions of BmVta1 and BmVps4 are highly up-regulated during silkworm metamorphosis and embryogenesis but down-regulated during larva stages, and are of higher levels in head, silk gland and testis than in Malpighian tube, fat body and ganglion, indicating important and similar roles of them in silkworm development and in silkworm tissues and organs. However, compared to BmVps4, the transcription of BmVta1 changes less drastically during development and is of much higher levels in midgut, ovary and hemolymph, suggesting the existence of distinct requirements of them in silkworm development and in certain tissues and organs.

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Xia H, Shao D, Liu X, Wang Q, Zhou Y, Chen K

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