PMID- 9663393
OWN - NLM
STAT- MEDLINE
DCOM- 19981001
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 8
IP  - 14
DP  - 1998 Jul 2
TI  - Phospholipase D1 localises to secretory granules and lysosomes and is 
      plasma-membrane translocated on cellular stimulation.
PG  - 835-8
AB  - Phospholipase D (PLD) activity has been implicated in the regulation of membrane 
      trafficking [1,2], superoxide generation and cytoskeletal remodelling [3,4]. 
      Several PLD genes have now been identified and it is probable that different 
      isoforms regulate distinct functions. Defining the subcellular localisation of 
      each isoform would facilitate understanding of their roles. Previous PLD 
      localisation studies have been based largely on enzyme activity measurements, 
      which cannot distinguish between isoforms [2,5]. We have cloned the cDNAs 
      encoding human PLD1a and PLD1b from an HL60 cell cDNA library and expressed them 
      as catalytically active fusion proteins with green fluorescent protein (GFP) in 
      COS-1 cells and RBL-2H3 cells, a mast cell model which degranulates upon 
      cross-linking of the high-affinity immunoglobulin E (IgE) receptor. In 
      unstimulated cells, GFP-PLD1b colocalised with secretory granule and lysosomal 
      markers; it was not found at the plasma membrane or nucleus and did not 
      colocalise with markers for the Golgi. Stimulation or RBL-2H3 cells through IgE 
      receptor cross-linking caused plasma membrane recruitment of GFP-PLD1b. 
      Inhibition of IgE-receptor-stimulated, PLD-catalysed phosphatidate formation 
      suppressed secretion of granule and lysosomal contents, but did not affect 
      translocation of GFP-PLD1b. These experiments suggest that PLD1 plays a role in 
      regulated exocytosis rather than endoplasmic reticulum (ER) to Golgi membrane 
      transport.
FAU - Brown, F D
AU  - Brown FD
AD  - Institute for Cancer Studies, Birmingham University Medical School, UK.
FAU - Thompson, N
AU  - Thompson N
FAU - Saqib, K M
AU  - Saqib KM
FAU - Clark, J M
AU  - Clark JM
FAU - Powner, D
AU  - Powner D
FAU - Thompson, N T
AU  - Thompson NT
FAU - Solari, R
AU  - Solari R
FAU - Wakelam, M J
AU  - Wakelam MJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Luminescent Proteins)
RN  - 0 (Receptors, IgE)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 3.1.4.4 (Phospholipase D)
RN  - EC 3.1.4.4 (phospholipase D1)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cell Membrane/enzymology
MH  - Cloning, Molecular
MH  - Cytoplasmic Granules/*enzymology
MH  - Golgi Apparatus/enzymology
MH  - Green Fluorescent Proteins
MH  - HL-60 Cells
MH  - Humans
MH  - Leukemia, Basophilic, Acute
MH  - Luminescent Proteins/biosynthesis
MH  - Lysosomes/*enzymology
MH  - Mast Cells/immunology/physiology
MH  - Phospholipase D/genetics/*metabolism
MH  - Rats
MH  - Receptors, IgE/physiology
MH  - Recombinant Fusion Proteins/biosynthesis/metabolism
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1998/07/15 00:00
MHDA- 1998/07/15 00:01
CRDT- 1998/07/15 00:00
PHST- 1998/07/15 00:00 [pubmed]
PHST- 1998/07/15 00:01 [medline]
PHST- 1998/07/15 00:00 [entrez]
AID - S0960-9822(98)70326-4 [pii]
AID - 10.1016/s0960-9822(98)70326-4 [doi]
PST - ppublish
SO  - Curr Biol. 1998 Jul 2;8(14):835-8. doi: 10.1016/s0960-9822(98)70326-4.