Suppression of transmitter release by Tat HPC-1/syntaxin 1A fusion protein.
It has been reported that the fusion protein with the protein transduction domain (PTD) peptide of HIV-1 Tat protein can be internalized through the cell membrane of intact cells, although the exact mechanism is unknown. In this report, we investigated whether this new method could be used for the molecular analysis of exocytosis via HPC-1/syntaxin 1A, which plays an important role in transmitter release. When applied to PC12 cells, Tat PTD fusion proteins were rapidly internalized into most cells. In order to show that the internalized protein remained biologically active, the H3 domain of HPC-1/syntaxin 1A was fused to Tat PTD (Tat-H3). Transmitter release in PC12 cells was suppressed by Tat-H3 treatment. These results indicate that the Tat fusion protein is a useful tool for analyzing the process of transmitter release.
Fujiwara
T
T
Department of Physiology, Kyorin University School of Medicine, Tokyo, Japan.
Yamamori
T
T
Akagawa
K
K
D000818:Animals; D000954:Antigens, Surface / Q000494:pharmacology*; D004705:Endocytosis / Q000502:physiology; D015696:Gene Products, tat / Q000494:pharmacology*; D008565:Membrane Proteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000494:pharmacology*; D018377:Neurotransmitter Agents / Q000378:metabolism*; D016716:PC12 Cells / Q000187:drug effects* / Q000378:metabolism; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D050600:SNARE Proteins; D050827:Syntaxin 1; D033921:Vesicular Transport Proteins
D000954:Antigens, Surface; D015696:Gene Products, tat; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents; D011993:Recombinant Fusion Proteins; D050600:SNARE Proteins; C494213:Stx1a protein, rat; D050827:Syntaxin 1; D033921:Vesicular Transport Proteins