Unconventional secretion of the mutated 19 kDa protein of Oplophorus luciferase (nanoKAZ) in mammalian cells

作者：Inouye Satoshi^*; Sato Jun ichi; Sahara Miura Yuiko; Hosoya Takamitsu; Suzuki Takahiro

来源：Biochemical and Biophysical Research Communications, 2014, 450(4): 1313-1319.

DOI：10.1016/j.bbrc.2014.06.140

• Amino-terminal signal peptide
• ER/Golgi-dependent secretion
• Brefeldin A
• Bioluminescence imaging

The putative amino-terminal signal peptide of the catalytic 19 kDa protein (KAZ) of Oplophorus luciferase was found to be a functional secretory peptide in mammalian cells. A 16 amino acid substituted mutant of KAZ (nanoKAZ) could be secreted from mammalian cells using the amino-terminal signal peptide of KAZ, but KAZ could not be secreted at all. Notably, nanoKAZ lacking the amino-terminal signal peptide could be secreted from mammalian cells, and the distribution of nanoKAZ on the cell membrane was confirmed by video-rate bioluminescence imaging. Thus, nanoKAZ lacking the amino-terminal signal peptide was expressed in the cytoplasm, translocated to the cell membrane, and released into the culture medium through an endoplasmic reticulum-Golgi-independent pathway.

• 出版日期2014-8-8