CHARACTERIZATION OF ADAPTOR PROTEIN COMPLEX-1 IN THE SILKWORM, Dombyx mori

摘要

To investigate the function of adaptor protein complex-1 (AP-1) in the silkworm, we characterized AP-1 in the silkworm by RJSAi technique and co-localization methods. As a result, A/J-7 was found to exist as cytosolic form and membrane-bound form distinguished by phosphate status, showing motecular mass difference. There was relatively more cytosolic form ofAl'-l than its membrane-bound counterpart in the silkworm. However, AP-1 distributed predominantly as cytosolic form in BmJS cells. Interruptionof AP-1 expression via DsRJSA was more efficient in BmJS cells than in the insect larval, which ted to a tendency to dissociation between subcellular organellas like the Colgi. apparatus and the mitochondria. Environmental condition changes like relatively higher temperature and treatment with dimethyl sulfoxide can tead to expression variance ofAl'-l both in mRJSA and protein level. In BmJS cells, both the heavy chain y and light chain a could cteariy co-localize with AP-1 beta, mostly formingpits in cytoplasm. Two isoforms of AP-1 a corresponded to distinct subcellular distribution pattern, possibly due to C-terminal amino acids difference.