Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells.
about
Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKINDynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sitesTranslocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase CIdentification and characterization of a novel human type II diacylglycerol kinase, DGK kappaA ceramide-binding C1 domain mediates kinase suppressor of ras membrane translocationRole of phosphatidic acid in the coupling of the ERK cascade.Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cellsAutoregulation of the Raf-1 serine/threonine kinaseRole of the autotaxin-lysophosphatidate axis in cancer resistance to chemotherapy and radiotherapyFull-length p40phox structure suggests a basis for regulation mechanism of its membrane bindingDiacylglycerol Kinases in T Cell Tolerance and Effector FunctionDiacylglycerol kinase θ couples farnesoid X receptor-dependent bile acid signalling to Akt activation and glucose homoeostasis in hepatocytesThe pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor suppressor in the lungProtein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactionsTAPAS-1, a novel microdomain within the unique N-terminal region of the PDE4A1 cAMP-specific phosphodiesterase that allows rapid, Ca2+-triggered membrane association with selectivity for interaction with phosphatidic acid14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domainPhospholipases of mineralization competent cells and matrix vesicles: roles in physiological and pathological mineralizationsPLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulationModulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acidPhospholipase D and phosphatidic acid-mediated generation of superoxide in ArabidopsisThe ankyrin repeat-containing adaptor protein Tvl-1 is a novel substrate and regulator of Raf-1Antigen-stimulated activation of phospholipase D1b by Rac1, ARF6, and PKCalpha in RBL-2H3 cellsCloning of a novel human diacylglycerol kinase (DGKtheta) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain.An intracellular motif of GLUT4 regulates fusion of GLUT4-containing vesicles.A-RAF kinase functions in ARF6 regulated endocytic membrane traffic.The role of G proteins in insulin signalling.Signal integration by lipid-mediated spatial cross talk between Ras nanoclustersRas membrane orientation and nanodomain localization generate isoform diversityAmphitropic proteins: regulation by reversible membrane interactions (review).Lysophosphatidic acid acyltransferase β (LPAATβ) promotes the tumor growth of human osteosarcoma.14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo.Membrane-binding and activation of LKB1 by phosphatidic acid is essential for development and tumour suppression.Docosahexaenoic acid: a positive modulator of Akt signaling in neuronal survivalPhospholipase D is involved in myogenic differentiation through remodeling of actin cytoskeleton.Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides.Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation.Quantitative in vivo fluorescence cross-correlation analyses highlight the importance of competitive effects in the regulation of protein-protein interactionsPhosphatidic acid mediates activation of mTORC1 through the ERK signaling pathway.Putting the pH into phosphatidic acid signalingTight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid.
P2860
Q24297523-E0624DD7-B0B1-4B0F-8082-E8664F00B946Q24302442-A2224847-C2CF-429D-A090-1B09A9D4C913Q24337455-84BCBAA3-2A1D-48BF-B176-6D41D2B40A40Q24337754-686B157E-5656-4F87-B613-9B62DED6C151Q24608466-A85A6CFF-763E-4CB5-9198-5FA102A878C7Q24643389-1BAB2E2D-A3A6-48B6-8F17-4D5E110C7193Q24651630-20153132-CC48-451D-A390-E3C811EA3DDEQ24684153-16FF026C-03E0-4924-91B0-EC11C58B2945Q27015257-50E124B0-37E7-4585-8D64-5F34E0441538Q27643779-B1A2333B-5BF5-4B91-A19B-53532D1036C6Q28079616-A9A88424-2523-4194-8F76-89F0975C9FB5Q28114796-2B1958DC-3E28-4574-97F8-D6A66819489CQ28188823-1CF33D83-7CF3-4F58-BA9F-984DA6153AE2Q28211695-36E03392-6656-458C-9E2E-29E851B8B1C9Q28216705-44039880-1E5D-4DB3-B0E5-2794CAF65C91Q28246442-F4CEEB1B-5366-40C9-BD3D-FB7C63F11320Q28286551-B6B6018B-77F2-4803-9662-2E3C3BA45B76Q28290445-C4911316-2458-4FD1-956E-334DC2B56B98Q28301067-BEFBE3B6-9296-4CAF-A4D6-9F72F30E49ACQ28345875-994EA756-E263-4727-AD11-B06DFFF2E21EQ28512234-107ACDF6-C11F-4186-850E-F9E57BC89775Q28579419-E4E4D1E7-15D6-4EA6-9BCE-E45270A3E605Q30176572-704F6011-3473-4D65-AC2D-E88142841B1BQ33336220-6D9BCB20-B5B6-48C2-AF57-67F3991FB5DAQ33413060-127F0BFA-4C3D-4E1B-A74B-B640E4C8686EQ33599408-EC96FCE3-50F2-4B67-83BE-2C3F0D44D53CQ33623159-2540930F-74A3-4A67-AA1D-F089BC9D5D8CQ33667116-9CB0F449-DA4F-4641-80D5-70AA7945F895Q33741843-B241A8B2-8500-40D9-9E05-5D0C4895BB84Q33769959-450CF9AE-52DF-4EB1-BB88-B6FFFB090BBBQ33774875-150ECACD-664A-4EE9-ADC0-47C54B438701Q33851000-EE01FC14-F20B-41DE-A0DF-6F1CF6C78C9AQ33911514-0147446F-3C55-4B37-B9F0-B612816C5675Q33913791-5DE64AB2-C4B8-4398-93B0-2EB95153C8D5Q34004482-AB985137-7F16-48C7-8E64-572CC25C7007Q34045664-B9A16770-588E-405F-AF2C-99BB29823C01Q34056400-9A38C75A-ABE9-4D9B-9DB7-A2F2003ACF0BQ34085728-00CEF588-433C-42EC-B124-9ECD37ECBFDEQ34089359-AE50197C-E5E1-4D70-8C61-FE6CB9B7DA5DQ34115185-A1AAC43C-7968-4D48-826C-2622F7DBECDB
P2860
Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Raf-1 kinase possesses distinc ...... din-Darby canine kidney cells.
@en
type
label
Raf-1 kinase possesses distinc ...... din-Darby canine kidney cells.
@en
prefLabel
Raf-1 kinase possesses distinc ...... din-Darby canine kidney cells.
@en
P2093
P2860
P356
P1476
Raf-1 kinase possesses distinc ...... din-Darby canine kidney cells.
@en
P2093
P2860
P304
P356
10.1074/JBC.271.14.8472
P407
P577
1996-04-01T00:00:00Z