Author:

Keywords:

Antigens, CD4, Biological Transport, Cell Line, Cell Membrane, Clathrin, Coatomer Protein, Dose-Response Relationship, Drug, Endoplasmic Reticulum, Endosomes, Fluorescent Antibody Technique, Glutathione Transferase, Glycoproteins, Hela Cells, Humans, Membrane Glycoproteins, Membrane Proteins, Phosphorylation, Precipitin Tests, Protein Kinase C, Protein Transport, Recombinant Proteins, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S., Temperature, Time Factors, Transfection, Viral Envelope Proteins, trans-Golgi Network, Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Cell Biology, PLASMA-MEMBRANE, ENDOPLASMIC-RETICULUM, LIVING CELLS, BREFELDIN-A, C FAMILY, COMPARTMENT, ACTIVATION, COMPLEX, YEAST, STACK, CD4 Antigens, HeLa Cells, 06 Biological Sciences, 11 Medical and Health Sciences, Developmental Biology, 31 Biological sciences, 32 Biomedical and clinical sciences

Abstract:

When a kinase inactive form of Protein Kinase D (PKD-K618N) was expressed in HeLa cells, it localized to the trans-Golgi network (TGN) and caused extensive tubulation. Cargo that was destined for the plasma membrane was found in PKD-K618N-containing tubes but the tubes did not detach from the TGN. As a result, the transfer of cargo from TGN to the plasma membrane was inhibited. We have also demonstrated the formation and subsequent detachment of cargo-containing tubes from the TGN in cells stably expressing low levels of PKD-K618N. Our results suggest that PKD regulates the fission from the TGN of transport carriers that are en route to the cell surface.