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results represent the first evidence that Pak1 links extracellular signals to the genetic cascade of transcription factors necessary for cranial neural crest specification
These findings expand the role of phosphoinositides in kinase signaling and suggest how altered phosphoinositide metabolism may upregulate Pak1 activity in cancer cells.
The data suggest that EphA4 activation sequesters active Cdc42 and in this way down-regulates cell-cell adhesion.
Pak1 inhibition interferes with the guidance of mesendoderm migration by directional cues residing in the extracellular matrix of the blastocoel roof, and with mesendoderm translocation in the embryo.
CYK4 inhibits Rac1-dependent PAK1 and ARHGEF7 effector pathways during cytokinesis.
microRNA-96 protects pancreatic beta-cell function by targeting PAK1 in gestational diabetes mellitus.
PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions.
PAK1 gene silencing decreases proliferation of MHCC97-H cells, HepG2 cells and cells in xenograft tumor through the p53/p21 pathway.
PAK1 silencing attenuated cell cycle progression, inducing apoptosis. Inhibition of PAK1 expression reduced tumor sizes and masses by modulating CREB expression and activation.
Once activated, c-Abl kinase regulated the activity of Vav1, which further affected Rac1/PAK1/LIMK1/cofilin signaling pathway.
The nuclear functions of PAK1 and its role in the regulation of DNA damage repair is reviewed.
PAK1 is upregulated in cutaneous T cell lymphoma. PAK1 silencing induced apoptosis and inhibited cell growth by stimulating the expression of PUMA and p21.
Results show that JMJD6 regulates the alternative splicing of PAK1 in melanoma cells.
PAK1 expression, evaluated by immunohistochemistry, was positively correlated with pERK and beta-catenin expression in lung tumors. Patients with high-PAK1, high-pERK, and high-nuclear beta-catenin tumors more frequently showed an unfavorable response to cisplatin-based chemotherapy when compared to their counterparts.
PKC-zeta may be responsible for the abnormal growth, proliferation, and migration of metastatic LOVO colon cancer cells via PKC-zeta/Rac1/Pak1/beta-Catenin pathway.
High expression of PAK1 is associated with invasion of gastric cancer.
Molecular modelling studies of PAK1 with its major interacting partners RHOA and STAT3 revealed potential network gene elements in breast invasive carcinoma.
miR4855p reverses EMT and promotes cisplatin-induced cell death by targeting PAK1 in oral tongue squamous cell carcinoma. This study suggests that PAK1 plays an essential role in the progression of OSCC and it is a potential therapeutic target for OSCC.
Because reduced PAK1 activity impaired FA/BRCA function, inhibition of this kinase in PAK1 amplified and/or overexpressing breast cancer cells represents a plausible strategy for expanding the utility of PARP inhibitors to FA/BRCA-proficient cancers.
Overall, the authors find that p27 directly promotes cell invasion by facilitating invadopodia turnover via the Rac1/PAK1/Cortactin pathway.
Results show that Pak1 is overexpressed in breast cancer cells and tissues, and found that Pak1 is a hormone responsive gene, whose expression can be modulated by steroid hormones, estrogen (E2) and progesterone (P4). Pak1 promoter analysis showed that PR mediates promoter activity via its binding to PRE present on the Pak1 promoter.
PAK1 confers TKI resistance in EGFR-mutant cells as well as in EGFR-wild-type cells.
Our findings offer an insight for the new drug development of PAK1 inhibitor. We also provide a possible explanation for the phenomenon that the application of the chlorhexidine in peritoneal lavage inhibited the development of tumor.
To our knowledge, this is the first study illustrating the mechanistic role of Pak1 in causing gemcitabine resistance via multiple signaling crosstalks, and hence Pak1-specific inhibitors will prove to be a better adjuvant with existing chemotherapy modality for pancreatic ductal adenocarcinoma (PDAC)
Furthermore, pharmacological inhibition of PAKs decreases ATXN1 levels in a mouse model of SCA1. To explore the potential of using PAK inhibitors in combination therapy, we combined the pharmacological inhibition of PAK with MSK1, a previously identified modulator of ATXN1, and examined their effects on ATXN1 levels. We found that inhibition of both pathways results in an additive decrease in ATXN1 levels.
Results provide evidence for a specific role of PAK1 in skin melanogenesis, despite of the fact that its expression level is minute: shRNA-induced silencing of PAK1 gene in melanocytes (B16F10) derived from mouse melanoma significantly reduced the alpha-MSH/IBMX-inducible melanogenesis to the basal level, while over-expression of PAK1 gene boosted the alpha-MSH-inducible melanogenesis without affecting the basal.
Serine/threonine-protein kinase proteins, also known as P21-activated kinase (PAK), and the mechanosensitive factor, Yes-associated protein 1 (YAP-1) are core mediators of pro-fibrotic integrin beta-1 signaling.
activated Pak1 regulates chromatin condensation by promoting H3 Ser(10) phosphorylation in oocytes after the resumption of meiotic progression
Depletion of active PAK1 up-regulates the immune system of APC(14/+) mice and suppresses intestinal tumour development. These observations suggest an important role for PAK1 in the immune response to tumours.
Results from our analysis showed that Pak1 overexpression, knockdown and Pak1 knockout cell line models showed that Pak1 confers protection to keratinocytes from UV-B-induced apoptosis and DNA damage via ATR
These results establish a novel signaling process whereby PAK1 upregulates COX-2, reduces anandamide levels and restricts tonic endocannabinoids-mediated processes.
The findings suggest that PAK1 deficiency may underlie an increased diabetic susceptibility. Discovery of ways to remediate glycaemic dysregulation via altering PAK1 or its downstream effectors offers promising opportunities for disease intervention.
present work presents the correlation between DSCAM gene overexpression and a dysregulation of the PAK pathway, resulting in altered morphological parameters of neuronal plasticity in the trisomic cell line, namely decreased number and length of processes
These results identify Pak1 and Pak2 as redundant regulators of myoblast differentiation in vitro and in vivo and as components of the promyogenic Ncad/Cdo/Cdc42 signaling pathway.
PAK-mediated phosphorylation of PKD1 at Ser203 triggers its membrane dissociation and subsequent entry into the nucleus, thereby regulating the phosphorylation of PKD1 nuclear targets, including class IIa histone deacetylases.
These results implicate PAK1 as a regulator of Pancreatic stellate cells activation, proliferation and apoptosis. Targeting stromal PAK1 could increase therapeutic response and survival of patients with pancreatic cancer.
The authors conclude that PAK1, besides its role in virus entry, also plays a relevant role in vaccinia virus dissemination.
PAK1 contributes to initiation of intestinal carcinogenesis
Pak1 is essential for adaptive physiological exercise-induced cardiac remodelling and support previous evidence that demonstrates Pak1 signalling is important for cardiac growth and survival.
Further investigations identified Pak1-ERM as a downstream signaling cascade upon Rac1 activation in the luminal epithelium necessary for uterine receptivity...Rac1 via P38 MAPK signaling ensures timely epithelial apoptotic death at postimplantation.
Nischarin inhibits neurite outgrowth by blocking PAK1 activation in neurons.
results indicate that NCAM is delivered to the cell surface through a kinesin-1-mediated transport mechanism in a PAK1-dependent manner.
propose that by repressing Pak1 expression, Rb prevents Rac1 hyperactivity usually associated with cancer and related to cytoskeletal derangements that disrupt cell adhesion, consequently enhancing cancer cell migratory capacity
FOXO-Pak1 pathway was recently shown to regulate mammalian neuronal polarity, our findings indicate that the roles of FOXO and Pak1 in neuronal migration are most likely conserved from C. elegans to higher organisms.
PAK1 promotes reproduction, whereas it inactivates HSP16.2 gene and shortens lifespan.
Pak-1 interacts with Wnt signaling to regulate tissue polarity and gene expression.
only PAK-1 functions in the GIT/PIX/PAK pathway independently of RAC/CDC42 GTPases.
Data show that combined loss of ROCK and PAK, or ROCK and MRCK, completely prevented embryonic elongation, but a constitutively active form of MLC-4 could only rescue a lack of MRCK.
This gene encodes a family member of serine/threonine p21-activating kinases, known as PAK proteins. These proteins are critical effectors that link RhoGTPases to cytoskeleton reorganization and nuclear signaling, and they serve as targets for the small GTP binding proteins Cdc42 and Rac. This specific family member regulates cell motility and morphology. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
p21 GTPase-associated kinase 1
, p21-activated kinase 1
, p21/Cdc42/Rac1-activated kinase 1 (STE20 homolog, yeast)
, putative CDKN1A-activated kinase 1
, STE20 homolog, yeast
, p21/Cdc42/Rac1-activated kinase 1 (yeast Ste20-related)
, serine/threonine-protein kinase PAK 1
, CDC42/RAC effector kinase PAK-A
, activated protein kinase alpha
, p21 (CDKN1A)-activated kinase 1
, protein kinase MUK2