The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing
about
An unappreciated role for RNA surveillanceThe CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1BNuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactionsPhosphorylation of CLK2 at serine 34 and threonine 127 by AKT controls cell survival after ionizing radiationPSKH1, a novel splice factor compartment-associated serine kinaseProcessive phosphorylation of alternative splicing factor/splicing factor 2Adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1Regulation and substrate specificity of the SR protein kinase Clk/StyComparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi.Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein PhosphorylationCloning of human PRP4 reveals interaction with Clk1Novel SR-rich-related protein clasp specifically interacts with inactivated Clk4 and induces the exon EB inclusion of ClkMass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/StyThe cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylationDigoxin suppresses HIV-1 replication by altering viral RNA processingCdc2-like kinase 2 is an insulin-regulated suppressor of hepatic gluconeogenesisIdentification of distant drug off-targets by direct superposition of binding pocket surfacesDAP-like kinase interacts with the rat homolog of Schizosaccharomyces pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G2/M phase transition.Failure to proliferate and mitotic arrest of CDK11(p110/p58)-null mutant mice at the blastocyst stage of embryonic cell developmentDetailed characterization of the mouse embryonic stem cell transcriptome reveals novel genes and intergenic splicing associated with pluripotencyConserved proline-directed phosphorylation regulates SR protein conformation and splicing functionPhosphorylation of the alternative mRNA splicing factor 45 (SPF45) by Clk1 regulates its splice site utilization, cell migration and invasion.The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation siteDevelopment of an orally available inhibitor of CLK1 for skipping a mutated dystrophin exon in Duchenne muscular dystrophySR protein kinases: the splice of life.The protein kinase Clk/Sty directly modulates SR protein activity: both hyper- and hypophosphorylation inhibit splicing.Detained introns are a novel, widespread class of post-transcriptionally spliced introns.Chemical treatment enhances skipping of a mutated exon in the dystrophin gene.Differential effect of CLK SR Kinases on HIV-1 gene expression: potential novel targets for therapy.Stress-responsive maturation of Clk1/4 pre-mRNAs promotes phosphorylation of SR splicing factor.Splicing changes in SMA mouse motoneurons and SMN-depleted neuroblastoma cells: evidence for involvement of splicing regulatory proteins.Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells.Latent herpes simplex virus infection of sensory neurons alters neuronal gene expression.CDK13, a Kinase Involved in Pre-mRNA Splicing, Is a Component of the Perinucleolar Compartment.Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivoPhosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors.Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phosphorylation-regulated (Dyrk) kinases: development of chemical probe ML315.Cdc2-like kinase 2 is a key regulator of the cell cycle via FOXO3a/p27 in glioblastomaCdc2-like kinase 2 suppresses hepatic fatty acid oxidation and ketogenesis through disruption of the PGC-1α and MED1 complex.Beyond ATM: the protein kinase landscape of the DNA damage response.
P2860
Q21092884-9C5BCC61-53D6-4412-9184-4D86A2192679Q22010528-873C3163-0E72-4491-9B5B-1091C19EF411Q24291592-3E9BF541-D8FB-4A3F-B9B3-4395C7A9C36AQ24294362-8CB59040-4855-4AFE-8228-5CDE262315F3Q24540428-B2C7D6F8-B6D3-482D-8955-002FDED897B7Q24647623-2C524843-DB0D-449D-AE1B-1CAE04E2D46BQ24657372-02B4F55B-0315-4F20-AE6F-B3E0869CEA8BQ24675674-0BF3701D-F610-452A-B928-F5F4B1D5855EQ24815881-781D3BDD-A023-4DAA-9678-3C6EBD01D6F1Q27654063-09C871E0-F8DA-4EB8-8751-E472174DE4FFQ28202917-27754C01-B32E-4D68-ACD7-B4578E0EFB33Q28217290-E3576F99-5D57-4F7F-BF9B-C1D7A2BE2466Q28276922-938E1761-940C-4E04-A352-3A4AD7CA98CCQ28291347-BEAF6A84-43D7-4974-A586-DF924E6949F2Q28489086-92A55BB1-7137-433A-94EE-3A5B7D29CCDBQ28511396-777BE55C-6F2D-4160-9EDA-4D2879C4F12DQ28538129-96B6C2C7-28FE-40F6-8F80-EE53A53FF01AQ28575564-4535E960-1A09-46C3-97BB-C99315C28FC7Q28585216-84D4AA1D-0EF8-4ED4-9B83-7F4AB90700C7Q28593426-414E6BD1-CA13-4B83-9E27-740C8D28DC92Q28822425-77587ED8-9193-4DB2-BA40-2AF9F0E0FA8FQ30419430-C77C70C8-D449-41F5-8F00-A9C0FC19D604Q33235281-6FE8B729-B481-4CCD-815E-14AF03C27F48Q33737691-FBAFB976-3806-4B79-84C3-05228EA9B4E4Q33765350-46073E6A-3AC2-4627-955D-EA69692CC704Q33959780-F8C03397-29A5-40C7-AFD5-7B97B0012453Q34799985-769213CE-1762-48D2-AB36-2963CE477EC1Q35039875-56CC0507-8531-4B03-B263-3B3A0F959D0EQ35143725-EE60408D-6695-45F3-A2C5-3D9A37621122Q35276828-0C0F922F-78D1-4DDC-B6FE-AEF261896B5BQ35563254-09FAC4C2-E5ED-4E22-9463-4199AAEA9791Q35695216-CB5B7EC2-7669-4B0A-8FFB-28586AA99ED9Q35803233-FCA08C69-7F17-4B09-BF80-10F1906BC9D1Q35926149-75CBD437-3924-44D7-B77E-E3B43F270EFAQ36255596-65EFC471-EA04-4D3E-9D94-9051C2F5B79CQ36342149-94047B08-9FBE-4369-A837-04EA174B7218Q36876032-056345B5-21E1-4483-9A3C-1B3E994BDFE7Q37295800-0EE390B1-8380-48E5-AD4D-BCC594C27BABQ37715596-FD76272C-F857-4DBE-B338-0C26F04BD116Q37875377-946F1BE1-73E7-416A-94CC-1EEC67CF9A1B
P2860
The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
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
name
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@ast
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en-gb
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@nl
type
label
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@ast
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en-gb
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@nl
prefLabel
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@ast
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en-gb
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@nl
P2093
P921
P3181
P356
P1476
The Clk2 and Clk3 dual-specifi ...... nd influence pre-mRNA splicing
@en
P2093
P3181
P356
10.1006/EXCR.1998.4083
P407
P577
1998-06-15T00:00:00Z