The hydrophobic segment of Arabidopsis thaliana cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes.
Diacylglycerol kinases (DGKs) catalyze the phosphorylation of diacylglycerol into phosphatidic acid. To fulfill their role in many signalling processes, DGKs must be located at, or in, membranes. Most mammalian DGKs are cytosolic and are recruited to membranes upon stimulation, except for epsilon type DGKs that are permanently membrane-associated through a hydrophobic segment. Nothing is known about the mechanism(s) involved in the membrane localization of plant DGKs. By fusion to fluorescent proteins, we show that two DGKs from cluster I in Arabidopsis thaliana possess amino-terminal hydrophobic segments that are sufficient to address them to endoplasmic reticulum membranes.
Vaultier
Marie-Noëlle
MN
UPMC Univ Paris 06, UMR 7180, Physiologie Cellulaire et Moléculaire des Plantes, F-94200 Ivry-sur-Seine, France.
Cantrel
Catherine
C
Guerbette
Françoise
F
Boutté
Yohann
Y
Vergnolle
Chantal
C
Ciçek
Dominique
D
Bolte
Susanne
S
Zachowski
Alain
A
Ruelland
Eric
E
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D017124:Conserved Sequence; D019852:Diacylglycerol Kinase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D057927:Hydrophobic and Hydrophilic Interactions; D007425:Intracellular Membranes / Q000201:enzymology*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
D019852:Diacylglycerol Kinase