The hydrophobic segment ofArabidopsis thalianacluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes

Autor: F. Guerbette, Eric Ruelland, Catherine Cantrel, Alain Zachowski, Dominique Çiçek, Chantal Vergnolle, Susanne Bolte, Marie-Noëlle Vaultier, Yohann Boutté
Přispěvatelé: Université Pierre et Marie Curie - Paris 6 (UPMC), Umeå University, Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2008
Předmět:
0106 biological sciences
Diacylglycerol Kinase
Molecular Sequence Data
Arabidopsis
Biophysics
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
Endoplasmic Reticulum
GFP
01 natural sciences
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
DIACYLGLYCEROL KINASES
Structural Biology
Genetics
Arabidopsis thaliana
Amino Acid Sequence
INTEGRAL PROTEIN
Phosphatidylinositol
Molecular Biology
Integral membrane protein
Conserved Sequence
030304 developmental biology
Diacylglycerol kinase
MEMBRANE SEQUESTERING
0303 health sciences
biology
Endoplasmic reticulum
ARABIDOPSIS THALIANA
Intracellular Membranes
Cell Biology
Phosphatidic acid
HYDROPHOBIC DOMAIN
biology.organism_classification
Protein Structure
Tertiary

Cell biology
Membrane
chemistry
Hydrophobic and Hydrophilic Interactions
010606 plant biology & botany
Zdroj: FEBS Letters
FEBS Letters, 2008, 582 (12), pp.1743-1748. ⟨10.1016/j.febslet.2008.04.042⟩
FEBS Letters, Wiley, 2008, 582 (12), pp.1743-1748. ⟨10.1016/j.febslet.2008.04.042⟩
ISSN: 0014-5793
1873-3468
Popis: International audience; 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 e 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.
Databáze: OpenAIRE