A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling.
about
Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase bindingGlyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathwaySRBC/cavin-3 is a caveolin adapter protein that regulates caveolae functionDifferential and regulated binding of cAMP-dependent protein kinase and protein kinase C isoenzymes to gravin in human model neurons: Evidence that gravin provides a dynamic platform for the localization for kinases during neuronal developmentCross-species sequence analysis reveals multiple charged residue-rich domains that regulate nuclear/cytoplasmic partitioning and membrane localization of a kinase anchoring protein 12 (SSeCKS/Gravin)A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated eventsMetastasis suppressor genes at the interface between the environment and tumor cell growthp32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; interaction and cellular localization of P32-PKC complexes in ray hepatocytesCharacterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase CSSeCKS/Gravin/AKAP12 inhibits cancer cell invasiveness and chemotaxis by suppressing a protein kinase C- Raf/MEK/ERK pathway.Ethanol and protein kinase C.PKC-η-MARCKS Signaling Promotes Intracellular Survival of Unopsonized Burkholderia thailandensisProtein kinase C binding partners.High PKC alpha and low E-cadherin expression contribute to high migratory activity of colon carcinoma cells.Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation.Emerging Roles for SSeCKS/Gravin/AKAP12 in the Control of Cell Proliferation, Cancer Malignancy, and Barriergenesis.Control of protein kinase C activity, phorbol ester-induced cytoskeletal remodeling, and cell survival signals by the scaffolding protein SSeCKS/GRAVIN/AKAP12.Increased localization and substrate activation of protein kinase C delta in lung epithelial cells following exposure to asbestos.Pivotal Role of AKAP12 in the Regulation of Cellular Adhesion Dynamics: Control of Cytoskeletal Architecture, Cell Migration, and Mitogenic Signaling.Protein kinase C, an elusive therapeutic target?SSeCKS, a major protein kinase C substrate with tumor suppressor activity, regulates G(1)-->S progression by controlling the expression and cellular compartmentalization of cyclin D.Regulation of interleukin receptor-associated kinase (IRAK) phosphorylation and signaling by iota protein kinase C.Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular endothelial cells by bacterial lipopolysaccharide.Translocation of MARCKS and reorganization of the cytoskeleton by PMA correlates with the ion selectivity, the confluence, and transformation state of kidney epithelial cell lines.Changes of Src-suppressed C kinase substrate expression in cytokine induced reactive C6 glioma cellsRb-dependent cellular senescence, multinucleation and susceptibility to oncogenic transformation through PKC scaffolding by SSeCKS/AKAP12.Characterization of calreticulin as a protein interacting with protein kinase C.Molecular characterization of protein kinase C-alpha binding to lamin A.Identification of PSF as a protein kinase Calpha-binding protein in the cell nucleus.Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation.Protein kinase C delta (deltaPKC)-annexin V interaction: a required step in deltaPKC translocation and function.AKAP12 in astrocytes induces barrier functions in human endothelial cells through protein kinase Czeta.Developmental expression of the protein kinase C substrate/binding protein (clone 72/SSeCKS) in rat testis identification as a scaffolding protein containing an A-kinase-anchoring domain which is expressed during late-stage spermatogenesis.PKCeta associates with cyclin E/cdk2/p21 complex, phosphorylates p21 and inhibits cdk2 kinase in keratinocytes.The relationship between Src-suppressed C kinase substrate and β-1,4 galactosyltransferase-I in the process of lipopolysaccharide-induced TNF-α secretion in rat primary astrocytes.Protein Kinase C Regulates Integrin-induced Activation of the Extracellular Regulated Kinase Pathway Upstream of ShcPICOT: A Multidomain Protein with Multiple Functions
P2860
Q24291582-065499B6-ED4A-41B8-A8FD-2371CB721210Q24291938-55858A9C-FCC7-4AC2-89EF-59F647BDA059Q24317453-FA23B53A-3BEE-4437-A809-5CA9C6A9C021Q28186760-073F51CC-D4AD-4B25-A623-07338605CCDCQ28253483-EBEE8623-DAC8-4053-A425-A9185EF04AE5Q28301334-78FB3916-D886-4CD0-B789-405C424C2E6BQ28394526-A36ADE93-D374-4014-BA92-0D1FC1A92452Q28581064-4AB8137D-513B-4932-A53A-86C58F3676D6Q28581520-DA425DDA-427D-4CF2-A983-90887D057B6BQ30433235-255B8E43-DE1E-4A42-9499-D240805628A6Q33747340-87A1B170-04AF-4AAD-A39E-794DF142CDDCQ33770513-C73E54CF-BA79-474C-87F6-65257B13792BQ33843447-38DEE0C1-23D4-4864-ACC8-FFEC0D194681Q33937259-E962E2E2-E99B-453F-BBE2-099E7A9CE208Q34271543-CF636AAA-4C76-45E8-9707-F16DCCC8CD84Q34972774-31FF9503-CF46-4198-BC95-CC7BD01FCCDDQ35515316-739A4209-65A4-4B05-A17A-2B9A84C55BE7Q35747910-AF22FC32-5546-4189-9B44-27B549163E21Q36090763-2C32E9B9-5FF1-4915-A3A7-FB733786A258Q37141320-BC255D51-3F96-42F3-A99A-82AD68D759B0Q39455728-735434A0-C518-4EFD-8087-A217613A2E7AQ40605895-CA393859-0DC2-4520-82C7-AC1940418A0FQ40756344-F1082316-40CA-4E0B-B5A5-C14876728D80Q40933970-9AB4AA67-3486-4046-8A64-8A3CBA53AF02Q41333093-A2580EB5-3B26-4190-BD0C-B71FE2D5D7BBQ41912117-6CC7C894-8DCF-4ED1-A796-5BFE500E7844Q42995202-322ED8D9-60E5-48FF-A1AA-34F3C81C94BBQ44059994-854EFDF2-D6C8-4262-B8CC-72CCC813DAB4Q44060004-54D884A7-6383-4C84-B5AE-486F17A44009Q45195797-F7D02F99-AB24-4063-A3FA-BFAF91846DF4Q45953150-BD6190F4-B00D-407F-ACEA-8F9CFB90A4CAQ47786297-57F8637C-F73C-455D-981B-E273FE526058Q52174794-E8F40DA0-EF57-436F-8E1B-9DE824D09CDDQ52585729-B7895971-17C0-4259-8F5F-58D41179511CQ53247833-82F36646-C8A2-406C-B14E-5ADACC8D5A90Q58323655-B84022C6-F663-4A88-8D53-880C55580174Q58689406-047F9132-95B5-473D-B7C6-C6D89251D4FF
P2860
A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
A major, transformation-sensit ...... ed in cytoskeletal remodeling.
@en
type
label
A major, transformation-sensit ...... ed in cytoskeletal remodeling.
@en
prefLabel
A major, transformation-sensit ...... ed in cytoskeletal remodeling.
@en
P2093
P2860
P356
P1476
A major, transformation-sensit ...... ed in cytoskeletal remodeling.
@en
P2093
P2860
P304
19482-19489
P356
10.1074/JBC.273.31.19482
P407
P577
1998-07-01T00:00:00Z