The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
about
Cdc42-induced activation of the mixed-lineage kinase SPRK in vivo. Requirement of the Cdc42/Rac interactive binding motif and changes in phosphorylationDirect activation of mitogen-activated protein kinase kinase kinase MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2.Regulation of MTK1/MEKK4 kinase activity by its N-terminal autoinhibitory domain and GADD45 binding.Dynamic 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 sitesCAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motilityRaf family kinases: old dogs have learned new tricksMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsSerine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activationS338 phosphorylation of Raf-1 is independent of phosphatidylinositol 3-kinase and Pak3Ras-specific exchange factor GRF: oligomerization through its Dbl homology domain and calcium-dependent activation of RafThe leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and RafEndogenous, hyperactive Rac3 controls proliferation of breast cancer cells by a p21-activated kinase-dependent pathwayRACK1 targets the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to link integrin engagement with focal adhesion disassembly and cell motilityHepatitis B virus X protein stimulates the mitochondrial translocation of Raf-1 via oxidative stressp21-activated kinase signaling in breast cancerThe evolutionary history of effectors downstream of Cdc42 and Rac.Raf activation is regulated by tyrosine 510 phosphorylation in DrosophilaRaf-interactome in tuning the complexity and diversity of Raf function.Calcium/calmodulin-dependent protein kinase II (CaMKII) phosphorylates Raf-1 at serine 338 and mediates Ras-stimulated Raf-1 activation.TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loopThe mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activityA tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteinsMEKK1 binds raf-1 and the ERK2 cascade componentsAn evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKKPAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activationInteraction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactionsAkt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migrationB-Raf and Raf-1 are regulated by distinct autoregulatory mechanismsRheb inhibits C-raf activity and B-raf/C-raf heterodimerizationPAK1 kinase promotes cell motility and invasiveness through CRK-II serine phosphorylation in non-small cell lung cancer cellsPAK1 negatively regulates the activity of the Rho exchange factor NET1Specific role of the extracellular signal-regulated kinase pathway in angiotensin II-induced cardiac hypertrophy in vitroRegulation of Raf-1 activation and signalling by dephosphorylationRegulation of mitogen-activated protein kinases in cardiac myocytes through the small G protein Rac1Striatal microRNA controls cocaine intake through CREB signallingRabGEF1 is a negative regulator of mast cell activation and skin inflammationRaf kinase inhibitory protein regulates Raf-1 but not B-Raf kinase activationRaf kinase inhibitory protein regulates aurora B kinase and the spindle checkpointHierarchical scaffolding of an ERK1/2 activation pathway
P2860
Q22254031-2523F76B-77D2-4A12-9F16-6B19685795FDQ24292137-7C61A1F7-58D5-41FF-A43F-65CAF95D9403Q24299183-651EC249-4F8C-49C7-8033-AC4B3B252DC4Q24302442-4E4E6B39-A446-4EFD-A2A0-88D4B1E561AAQ24311778-3FFFBE3E-DC0E-4278-B6DA-D8860AB5B9ECQ24316181-767198B7-3707-4E93-AD0D-732262291823Q24532168-BDFDFB7E-0082-4034-8CEF-DEC6C2A124D9Q24534094-FF0B5436-3529-4883-B313-D32B23F578DDQ24550986-070F65E6-6B69-42CC-B880-3C9EE4B349A3Q24554485-555A9B4F-90FC-471E-9405-B459D5E06E04Q24607066-6EFC3107-B538-492D-86AD-51C769809894Q24649739-142ABA8B-9B08-43FB-AE2B-4271A9B4446EQ24681308-BCE68F60-B94A-412C-A1B6-F30E8ADDAA00Q24683035-901514BA-404B-4619-8DB9-E59BCB9F3F9CQ24796768-047FCF89-4086-42B7-82D0-C55838E43E9EQ24806492-86B29EDD-2741-4D0F-8E66-3DD20C45BDE2Q27333187-0CBDA972-A1B6-4E66-BEEA-FD6C69239277Q27692653-B570E700-129B-43C8-B0F3-9EF6325348F7Q27865262-18EC32F5-95B7-4943-B427-8E6670710DD3Q28115673-07864A09-1755-4C85-A7BF-EF4C61194EF9Q28118693-D10D837D-DD68-4FF2-AEDF-60BA7C956A5AQ28140881-F27E090E-41F1-4466-8443-1E57B6381E75Q28145204-147E4115-FBD6-4F6E-9D17-0AF3FC559A7AQ28185707-AA5879E3-CD51-47D9-BF59-B76332FCD83FQ28188974-BCEA0B3A-B8F7-47B1-BAC9-55E7E36B2113Q28208695-194D4985-628D-49E4-8C39-26B193D4CCCAQ28211695-3A264592-BD9F-4519-81F7-35637D409892Q28213453-780A06CD-E76A-4ECF-BD46-E2DD98D8BC51Q28235023-FB6E7303-D4A5-4488-A0A5-0A34282D1E69Q28248759-287F1756-C1C9-4193-A76F-5CC5990C3F0CQ28272164-4F470CE3-6DAC-4AFA-9B0C-802EBA057F6DQ28305198-380151BA-E16A-4D14-9D89-1EA53C28BA8FQ28344062-DD280487-ED94-4F56-A461-0DFEC76760C1Q28344727-1A1EB515-6D16-4969-B0F8-CAB2625F8111Q28346098-724FEC47-DC35-4046-96A7-0704B34D5184Q28397558-27D48E29-0287-4DDD-AE2D-8A84B642BB5AQ28513940-2E825266-9E56-4852-8E44-41AA6361FFB2Q28565091-1DB624E1-43A4-437C-B3B7-61312E02A648Q28567156-7816C733-5DAB-403D-9E51-B3CDB28991DCQ28578122-32A91AFA-C058-48F3-8FE6-D2F46154C70A
P2860
The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
description
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Nature
@fr
artículu científicu espublizáu en 1998
@ast
scientific journal article
@en
vedecký článok (publikovaný 1998/11/12)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/11/12)
@nl
наукова стаття, опублікована в листопаді 1998
@uk
مقالة علمية (نشرت في 12-11-1998)
@ar
name
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@ast
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@en
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@nl
type
label
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@ast
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@en
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@nl
prefLabel
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@ast
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@en
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@nl
P2093
P2860
P3181
P356
P1433
P1476
The protein kinase Pak3 positi ...... phosphorylation of serine 338
@en
P2093
A. J. King
D. Barnard
M. S. Marshall
S. Bagrodia
P2860
P2888
P304
P3181
P356
10.1038/24184
P407
P577
1998-11-12T00:00:00Z
P6179
1039223180