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DGKepsilon is detected in a filamentous pattern, parallel to the long axis of cell, and on actin stress fibers
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prior to cell attachment, phorbol ester induce translocation of DGKgamma from the cytoplasm to the cell periphery
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activity of DGK-I is recovered dominantly in the soluble fraction, that for DGK-II in the particulate fraction and that for DGK-III in soluble and particulate fraction
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cytoplasm at the early stage of culture, indicating that DGKgamma is transported from the cytoplasm to the nucleus
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prior to cell attachment, phorbol ester induce translocation of DGKgamma from the cytoplasm to the cell periphery
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DGKeta1 and DGKeta2 are rapidly translocated from the cytoplasm to endosomes in response to stress stimuli. DGKeta1 is rapidly relocated back to the cytoplasm upon removal of stress stimuli. DGKeta2 exhibits sustained endosomal association
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one variant of DGKbeta is associated with the plasma membrane, the other isoform is predominantly localized within the cytoplasm
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DGKiota
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isoform diacylglycerol kinase delta-1, but not a splice variant isoform diacylglycerol kinase delta-2 or the other type II isoform diacylglycerol kinase ny-1/2, translocates from the cytoplasm to the plasma membrane in HEK-293 and mouse myoblast C2C12 cells within 5 min in response to high glucose levels. The translocation is inhibited by phosphatidylinositol 3-kinase inhibitors, LY294002 and GDC-0941. The PH and C1 domains are responsible for the plasma membrane translocation and the sterile alpha-motif domain negatively regulates the translocation
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when osmotically shocked with 0.5 M sorbitol, isoform DGKeta4 is distributed in punctate vesicles in the cytoplasm
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DGK-zeta export from nucleus to cytoplasm is regulated by a leucine-rich nuclear export signal through the exportin chromosome regional maintenance protein 1
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in the basal state, DGKzeta resides in the cytoplasm, but upon appropriate cellular events, it translocates to different parts of the cell in order to perform its biological role
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isozyme alpha
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DGKiota immunoreactivity is distributed solely in the cytoplasm of most of the dorsal root ganglion
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co-localizes with actin filaments
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isoform DGKalpha is detected sparsely in the cytoplasm, in aortic smooth muscle cell contracted by serotonin DGKepsilon is detected diffusely in the cytoplasm without a filamentous stress fiber pattern
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localized in the narrow cytoplasmic space between smooth endoplasmic reticulum and plasma membrane
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isoform DGKzeta translocates from the nucleus to the cytoplasm inbeta-cells in response to a beta-cell-selective toxin streptozotocin
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DGK-II
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DGK-III
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no activity in cytosol
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isoenzyme DGK-I, DGK-II and DGK-II
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in lymphocytes the basal activity is 1.6fold higher in the membrane fraction than in cytosol. In neutrophils the basal activity is identical in cytosol and mambrane-fraction
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DGKalpha is a cytosolic enzyme that must relocate to the membrane in response to receptor stimulation to exercise its function
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DGKalpha is a cytosolic enzyme that must relocate to the membrane in response to receptor stimulation to exercise its function
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DGK I
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isozyme DGKgamma in hippocampal pyriamidal cells and proximal dendrites
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fusion constructs of Green Fluorescent Protein to truncated forms of diacylglycerol kinase 1 and diacylglycerol kinase 2 missing the catalytic and accessory domains
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DGKeta1 and DGKeta2 are rapidly translocated from the cytoplasm to endosomes in response to stress stimuli. DGKeta1 is rapidly relocated back to the cytoplasm upon removal of stress stimuli. DGKeta2 exhibits sustained endosomal association. Oligomerization of DGKeta2 mediated by its SAM domain is largely responsible for its sustained endosomal localization
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trans-Golgi network
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diacylglacerol kinase isoform gamma
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recruitment of diacylglycerol kinase alpha to the membrane is mediated both via its proline-rich sequence and phosphorylation of Y335
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bound to
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intrinsic membrane-protein
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rhabdomeral membrane, the enzyme is located predominantly in the cytoplasmic subrhabdomeral cisternae, a cytoplasmic membrane system located at close distance from the microvilli. Excised membrane patches retain a functional enzyme DGK
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rhabdomeral membrane, the enzyme is located predominantly in the cytoplasmic subrhabdomeral cisternae, a cytoplasmic membrane system located at close distance from the microvilli. Excised membrane patches retain a functional enzyme DGK
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integral membrane protein
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bound to
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tightly associated with the inner membrane
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the region of transmembrane helix 1 spanning the hydrophobic core of the bilayer runs from Glu28 on the cytoplasmic side to Asp49 or Val50 on the periplasmic side. This locates the charged/polar cluster 32RQE34 within the hydrophobic core of the bilayer. Hydrophobic matching between the protein and the surrounding lipid bilayer is highly efficient
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the enzyme is an integral membrane protein
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in lymphocytes the basal activity is 1.6fold higher in the membrane fraction than in cytosol. In neutrophils the basal activity is identical in cytosol and membrane-fraction
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the hydrophobic domain of DGKepsilo does not contribute to substrate specificity but plays a role in permanently sequestering the enzyme to a membrane
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segment from amino acid residues 18 to 42 forms a bent helix that enters and leaves the same side of the membrane
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upon activation of T lymphocytes, diacylglycerol kinase alpha is phosphorylated, and the phosphoprotein is located at the plasma membrane
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DGKalpha is a cytosolic enzyme that must relocate to the membrane in response to receptor stimulation to exercise its function
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at early stages of T cell immunological synapse formation, isoform zeta translocates rapidly to the plasma membrane
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sterile alpha-motif of diacylglycerol kinase delta1 forms helical polymers through a head-to-tail interaction. Disruption of polymerization by mutations constitutively localizes the enzyme to the plasma membrane
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DGKalpha is a cytosolic enzyme that must relocate to the membrane in response to receptor stimulation to exercise its function
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integral membrane protein
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bound to
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DGK IV
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mainly associated with internal membranes
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agonist-induced activity of nuclear DGKthata activity, nuclear localization of DGKdelta
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DGKiota
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DGK-theta is localized in the speckle domain of the nucleus
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involvement of isoform diacylglycerol kinase zeta in cell-cycle progression
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isoform diacylglycerol kinase zeta localizes to the nucleus during interphase including G1, S, and G2 phases in NIH-3T3 cells and in proliferating spermatogonia in the testis. Enzyme is associated with chromatin and dissociates from chromatin during mitotic phase
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a portion of intracellular DGKzeta protein is localized to the nucleus
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DGK-zeta displays a functional independent nuclear export signal sequence between the amino acid residues 362-370
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DGK-theta is localized in the speckle domain of the nucleus
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isozyme zeta
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DGKzeta is detected heterogeneously in the nucleus and cytoplasm of small neurons of the dorsal root ganglion with variable levels of distribution, whereas it is detected exclusively in the cytoplasm of large neurons
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a portion of intracellular DGKzeta protein is localized to the nucleus
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isoform DGKzeta is observed as a granular pattern in the nucleus, isoform DGKalpha is detected sparsely in the nucleus
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in bovine rod outer segments obtained from retinas under room light conditions, DAGKepsilon and type I DAGK activity is present. Isozyme DAGKepsilon appears to be higher in rod outer segments from bleached bovine retinas than in those under dark conditions
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from albino rats, isozyme DAGKepsilon appears to be higher in rod outer segments from rat retinas exposed to light than in those under dark conditions. DAGKepsilon in rat retina naturally exposed to room light is present in all retinal layers and is distributed along the photoreceptor cell
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from albino rats, isozyme DAGKepsilon appears to be higher in rod outer segments from rat retinas exposed to light than in those under dark conditions. DAGKepsilon in rat retina naturally exposed to room light is present in all retinal layers and is distributed along the photoreceptor cell
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the enzyme is an integral membrane protein, a trimer situated with half its bulk in the membrane and half in the cytosol
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one variant of DGKbeta is associated with the plasma membrane, the other isoform is predominantly localized within the cytoplasm
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isozyme alpha
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isoform diacylglycerol kinase delta-1, but not a splice variant isoform diacylglycerol kinase delta-2 or the other type II isoform diacylglycerol kinase ny-1/2, translocates from the cytoplasm to the plasma membrane in HEK-293 and mouse myoblast C2C12 cells within 5 min in response to high glucose levels. The translocation is inhibited by phosphatidylinositol 3-kinase inhibitors, LY294002 and GDC-0941. The PH and C1 domains are responsible for the plasma membrane translocation and the sterile alpha-motif domain negatively regulates the translocation
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when osmotically shocked with 0.5 M sorbitol, isoform DGKeta3 is partly translocated to the plasma membrane and co-localizes with the actin cytoskeleton
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isozyme alpha
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activation and relocalization to plasma membrane of DGKalpha is a direct consequence of PI3K activation
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isozyme DGKbeta predominantly, in hippocampal pyriamidal neurons including perikarya and the peripheral dendrites, dendrit cell body
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active site of the enzyme is localized to the inner cytoplasmic surface
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rhabdomeral membrane, the enzyme is located predominantly in the cytoplasmic subrhabdomeral cisternae, a cytoplasmic membrane system located at close distance from the microvilli. Excised membrane patches retain a functional enzyme DGK
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rhabdomeral membrane, the enzyme is located predominantly in the cytoplasmic subrhabdomeral cisternae, a cytoplasmic membrane system located at close distance from the microvilli. Excised membrane patches retain a functional enzyme DGK
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activity of DGK-I is recovered dominantly in the soluble fraction, that for DGK-II in the particulate fraction and that for DGK-III in soluble and particulate fraction
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additional information
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subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
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additional information
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subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
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additional information
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subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
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additional information
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subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
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additional information
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subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
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additional information
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no isozyme DGKgamma in the nucleus, subcellular localization of isozymes in neurons
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additional information
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diacylglacerol kinase isoform epsilon is distributed around the perinuclear region
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additional information
diacylglacerol kinase isoform epsilon is distributed around the perinuclear region
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additional information
diacylglacerol kinase isoform epsilon is distributed around the perinuclear region
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additional information
diacylglacerol kinase isoform epsilon is distributed around the perinuclear region
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