| 1996 |
PKN (PKN1) directly binds to GTP-bound RhoA (but not GDP-RhoA) and is activated by this interaction both in vitro and in vivo, establishing PKN as a Rho effector serine/threonine protein kinase. |
Yeast two-hybrid cloning, in vitro binding assay, in vivo kinase activation assay |
Science |
High |
8571126
|
| 1999 |
Crystal structure of human RhoA complexed with the effector domain of PKN/PRK1 at 2.2 Å resolution reveals that the PKN effector domain adopts an antiparallel coiled-coil finger (ACC finger) fold that binds to RhoA switch I, beta strands B2/B3, and helix A5, predominantly via specific hydrogen bonds. |
X-ray crystallography at 2.2 Å resolution |
Molecular cell |
High |
10619026
|
| 1994 |
PKN kinase activity is activated several-fold by unsaturated fatty acids (arachidonic acid, linoleic acid, oleic acid) and by limited proteolysis with trypsin, but not by Ca2+/phosphatidylserine/diolein (the classical PKC activators). |
In vitro kinase assay with peptide substrates, limited proteolysis |
Biochemical and biophysical research communications |
High |
7945381
|
| 1995 |
Purified native PKN from rat testis is a 120 kDa serine/threonine kinase activated by unsaturated fatty acids and detergents; autophosphorylation activity is partially inhibited by alkaline phosphatase pretreatment, suggesting autophosphorylation contributes to activity. |
Protein purification (~8000-fold), in vitro kinase assay, alkaline phosphatase treatment |
The Biochemical journal |
High |
7654208
|
| 1996 |
The RhoA-binding region of PKN1 maps to amino acid residues 33–111 (with residues 74–113 critical for association); PKN1 binding to RhoA inhibits both endogenous and GAP-stimulated GTPase activity of RhoA, suggesting PKN1 can sustain the active GTP-bound form of RhoA. |
Yeast two-hybrid system, in vitro binding assay with truncation mutants, synthetic peptide competition, GTPase activity assay |
FEBS letters |
High |
8647255
|
| 1996 |
PKN1 associates with alpha-actinin via its N-terminal region (outside the RhoA-binding domain) binding to the third spectrin-like repeats of alpha-actinin; this interaction is regulated by Ca2+ for non-skeletal muscle type and is stimulated by phosphatidylinositol 4,5-bisphosphate for full-length alpha-actinin. |
Yeast two-hybrid, in vitro binding with truncation mutants, co-immunoprecipitation from COS7 cells |
The Journal of biological chemistry |
High |
9030526
|
| 1996 |
PKN1 associates with and phosphorylates the head-rod domain of all three neurofilament subunits (NF-L, NF-M, NF-H); phosphorylation of NF-L by PKN inhibits neurofilament polymerization in vitro. |
Yeast two-hybrid, in vitro binding, in vitro kinase assay with purified neurofilaments, polymerization assay |
The Journal of biological chemistry |
High |
8621664
|
| 1997 |
PKN1 phosphorylates vimentin and GFAP in their head domains in vitro, resulting in nearly complete inhibition of filament formation; the regulatory domain of PKN1 interacts with vimentin. |
Yeast two-hybrid, in vitro binding assay, in vitro kinase assay, filament formation assay |
Biochemical and biophysical research communications |
High |
9175763
|
| 1998 |
PKN is cleaved by caspase-3 (or a related caspase) at specific aspartate residues during apoptosis, generating a constitutively active catalytic fragment; site-directed mutagenesis of the cleavage sites prevented fragment generation, and the cleavage was inhibited by the caspase inhibitor DEVD-CHO. |
In vitro cleavage with recombinant caspase-3, site-directed mutagenesis, immunoblot in apoptotic cells |
Proceedings of the National Academy of Sciences of the United States of America |
High |
9751706
|
| 1999 |
The regulatory region of PKN1 (residues 455–511) contains an autoinhibitory domain that inhibits kinase activity in a substrate-competitive manner (Ki = 0.6 µM); arachidonic acid relieves autoinhibition by this segment. Phosphorylation at Thr64, Ser374, or Thr531 in the regulatory region and Thr774 in the activation loop are required for full kinase activity. |
Deletion mutagenesis in insect cells, in vitro kinase inhibition assay with recombinant peptide fragments, site-directed mutagenesis of phosphorylation sites |
Journal of biochemistry |
High |
10467162
|
| 1996 |
PKN1 translocates from the cytosol to the nucleus in response to heat shock (42°C), sodium arsenite, and serum starvation, and returns to the cytoplasm upon recovery from heat shock. |
Confocal immunofluorescence microscopy, subcellular fractionation, immunoblotting |
Proceedings of the National Academy of Sciences of the United States of America |
High |
8816775
|
| 2000 |
PKN1 phosphorylates tau protein at specific sites in microtubule-binding domains (Ser258, Ser320, Ser352), with Ser320 being PKN1-specific (not phosphorylated by PKC isoforms); PKN1 activation disrupts microtubule arrays in vitro and in vivo. |
In vitro kinase assay with tau peptides, site-directed mutagenesis, phospho-specific antibodies, transfection of active/inactive PKN in CHO cells |
The Journal of biological chemistry |
High |
11104762
|
| 2001 |
PKN1 delays mitotic timing by directly phosphorylating and inhibiting Cdc25C phosphatase activity, thereby delaying Tyr15 dephosphorylation of Cdc2 and entry into mitosis; active PKN causes cleavage arrest in Xenopus embryos and delayed mitosis in Xenopus cycling extracts. |
Xenopus embryo microinjection, Xenopus egg extract cell cycle assay, in vitro Cdc25C kinase/phosphatase assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
11134534
|
| 2001 |
PKN1 directly interacts with and stimulates the activity of phospholipase D1 (PLD1) in vitro and in vivo; PKNα binds residues 228–598 of PLD1 and stimulates PLD1 activity in the presence of PIP2. |
Co-immunoprecipitation from COS7 cells, in vitro binding with PLD1 deletion mutants, in vitro PLD1 activity assay |
The Journal of biological chemistry |
High |
11259428
|
| 2003 |
PKNα (PKN1) phosphorylates MLTKα (a MAPKKK) and enhances its kinase activity in vitro; PKNα associates with all components of the p38γ MAPK cascade (p38γ, MKK6, MLTKα), functioning as both an upstream activator and a scaffold for p38γ MAPK signaling. |
In vitro kinase assay, co-immunoprecipitation, SDS-PAGE mobility shift assay, dominant-negative expression |
Journal of biochemistry |
Medium |
12761180
|
| 2005 |
PKN1 (activated by TGF-β1 via RhoA) phosphorylates Cdc25C at Ser216, promoting 14-3-3 binding to Cdc25C and inactivating it, thereby delaying G2/M transition; PKN1 and Cdc25C coimmunoprecipitate and colocalize to the nucleus prior to mitosis. |
RNAi knockdown, constitutively active PKN1 expression, in vitro kinase assay on Cdc25C, phospho-specific Ser216 detection, co-immunoprecipitation, immunofluorescence colocalization |
Cell cycle |
High |
17374997
|
| 2005 |
PKN1 involvement in arsenite-induced G2/M delay is mediated by direct phosphorylation of Cdc25C at Ser216, which facilitates 14-3-3 association; a Cdc25C S216A phospho-mutant partially abrogated arsenite-induced cell cycle arrest. |
Constitutively active PKN1 expression in HeLa cells, in vitro kinase assay, Cdc25C S216A mutant expression, co-IP |
Molecular carcinogenesis |
High |
15791647
|
| 2006 |
Salmonella effector SspH1 interacts with PKN1 via its leucine-rich repeat (LRR) domain, and PKN1 expression decreases NF-κB-dependent reporter gene activity while PKN1 depletion by RNAi increases it, indicating PKN1 negatively modulates NF-κB signaling. |
Yeast two-hybrid screen, domain mapping of LRR-PKN1 interaction, RNAi knockdown, NF-κB reporter assay |
Cellular microbiology |
Medium |
16611232
|
| 2013 |
X-ray structure of SspH1–PKN1 complex reveals that the SspH1 LRR domain binds specifically to the HR1b coiled-coil subdomain of PKN1, sterically displacing the SspH1 catalytic domain to activate its E3 ubiquitin ligase activity; SspH1 catalyzes ubiquitination and proteasome-dependent degradation of PKN1 in cells, attenuating androgen receptor responsiveness. |
X-ray crystallography of SspH1–PKN1 complex, ubiquitination assay in cells, proteasome inhibitor experiments, androgen receptor reporter assay |
Molecular and cellular biology |
High |
24248594
|
| 2008 |
PKN1 phosphorylates TRAF1 in vitro and in vivo; this phosphorylation recruits TRAF1 to TNFR2 and is required for attenuation of constitutive NF-κB and JNK signaling; mutagenesis of the phospho-acceptor residue in TRAF1 abrogates PKN1-dependent TNFR2 recruitment. |
In vitro kinase assay, co-immunoprecipitation, RNAi, phospho-acceptor mutagenesis, NF-κB/JNK reporter assays |
Genes to cells |
High |
18429822
|
| 2004 |
PKN1 directly binds the TRAF domain of TRAF2 through a PXQX(S/T) motif (residues 580–584); mutation of this motif abrogates co-immunoprecipitation with TRAF2; RNAi knockdown of PKN1 reduces TRAF2-induced NF-κB activation. |
Yeast two-hybrid, in vitro binding with TRAF2 deletion mutants, co-immunoprecipitation, site-directed mutagenesis, RNAi, NF-κB reporter assay |
Biochemical and biophysical research communications |
Medium |
14741690
|
| 2010 |
PKN1 is activated by ischemia/reperfusion (phosphorylated at Thr774) in the heart; transgenic cardiac-specific overexpression of constitutively active PKN1 reduces infarct size and apoptosis, while dominant-negative PKN1 increases injury; PKN1 mediates phosphorylation of αB-crystallin and stimulates proteasome activity, partially accounting for cardioprotection. |
Transgenic mouse (cardiac-specific CA and DN PKN1), in vivo I/R model, TUNEL assay, immunoblot for αB-crystallin phosphorylation, proteasome activity assay, epoxomicin inhibition |
Circulation research |
High |
20595653
|
| 2011 |
PKN1 (PKNα) serves as a component of an AKAP-Lbc–assembled signaling complex containing RhoA effector PKNα, MLTK, MKK3, and p38α; this complex is required for α1b-adrenergic receptor-mediated RhoA-dependent activation of p38α MAPK, as silencing AKAP-Lbc specifically reduces this pathway. |
Co-immunoprecipitation, siRNA knockdown of AKAP-Lbc, p38α kinase activity assay, selective pharmacological dissection |
The Journal of biological chemistry |
Medium |
21224381
|
| 2008 |
A cleaved (caspase-activated) form of PKN1, but not wild-type PKN1, disrupts neurofilament organisation and axonal transport in neurons; PKN1 is cleaved and activated in SOD1G93A ALS model mice and in glutamate-treated neurons. |
Expression of cleaved vs. wild-type PKN1 in neurons, neurofilament transport assay, immunoblot for cleavage in transgenic mice and glutamate-treated cells |
FEBS letters |
Medium |
18519042
|
| 2011 |
PKN1 and PKN3 share a phosphorylation consensus motif requiring an arginine at position −3 and intolerance of arginine at position +1 (PKN1) or −1 (PKN3); PKN1 phosphorylates EGFR at Thr654 in vitro and this site is constitutively phosphorylated in a PKN-dependent manner in vivo. |
Peptide library substrate screen, protein array, site mutagenesis, in vitro kinase assay, cellular phosphorylation assay |
The Biochemical journal |
High |
21749319
|
| 2013 |
PKN1 inhibits Wnt/β-catenin signaling in melanoma cells; PKN1 is found in a protein complex with Frizzled 7 and co-purifying proteins by affinity purification/mass spectrometry; siRNA depletion of PKN1 enhances β-catenin reporter activity and increases WNT3A-induced apoptosis. |
siRNA screen, phosphoproteomics, affinity purification–mass spectrometry, β-catenin reporter assay |
The Journal of biological chemistry |
Medium |
24114839
|
| 2017 |
PKN1 phosphorylates RPH3A, which enhances binding of RPH3A to GTP-bound RAB21; this PKN1–RPH3A–RAB21 axis is required for polarized localization of RAB21 and PIP5K1C90 in neutrophils, integrin activation, and adhesion to endothelial cells; myeloid-specific loss of PKN1 decreases tissue injury in renal ischemia–reperfusion. |
In vitro kinase assay, co-immunoprecipitation, GTP-RAB21 pulldown, immunofluorescence of polarization, integrin activation assay, myeloid conditional KO mouse, renal I/R injury model |
Cell reports |
High |
28636945
|
| 2017 |
PKN1 kinase activity is regulated by TORC2-dependent phosphorylation of the turn motif (TM); amino acid substitution in the TM reduces kinase activity; PKN1 contributes to cell motility in human prostate cancer cells. |
TORC2-specific inhibitor (torin), phospho-TM-specific antibody, TM mutagenesis, in vitro kinase assay, cell motility assay, depletion approaches |
The Prostate |
Medium |
28875501
|
| 2018 |
Loss of PKN1 in vivo doubles myocardial infarct size after I/R; PKN1 co-localizes to the sarcoplasmic reticulum during ischemia and interacts with CamKIIδ; PKN1 loss increases basal CamKIIδ activation and phospholamban Thr17 phosphorylation, suggesting PKN1 limits CamKIIδ-dependent SR calcium dysregulation. |
PKN1 knockout mouse, Langendorff I/R perfusion, GC-MS/MS and immunoblot co-IP with CamKIIδ, PhosTag gel, confocal immunofluorescence, siRNA in NRVM |
Cardiovascular research |
High |
29045568
|
| 2017 |
PKN1 kinase activity is required for lymphocyte trafficking/egress from secondary lymphoid organs; knock-in mice with a PKN1 T778A kinase-dead mutation show lymphocyte sequestration in spleen and lymph nodes, reduced chemotaxis, and impaired S1P-directed migration in a cell-autonomous manner. |
Knock-in mouse (T778A mutation), cell transfer experiments, in vitro chemotaxis assay, flow cytometry |
Scientific reports |
High |
28794483
|
| 2014 |
PRK1/PKN1 regulates migration and gene expression in androgen-independent prostate cancer cells through its kinase activity; PKN1 interacts with scaffold protein SPAG9/JIP4 and this interaction is required for p38 phosphorylation and cell migration; a PKN1 inhibitor prevents metastases in mice. |
Sibling KD, transcriptome/interactome analysis, co-localization in tissue, p38 phosphorylation assay, cell migration assay, in vivo metastasis model with inhibitor |
Oncotarget |
Medium |
25504435
|
| 2020 |
PKN1 (specifically the PKN1a splice variant) promotes synaptic maturation by upregulating neuronal glutamate transporter EAAT3 expression; PKN1a knockout unmasks aberrant mGluR-dependent LTD and AMPA receptor silencing, and reduces glutamate uptake through EAAT3. |
PKN1a-specific knockout mouse, mGluR-LTD electrophysiology, glutamate uptake assay, silent synapse analysis, spine morphology |
Communications biology |
High |
33244074
|
| 2023 |
Overloading-activated RHOA–PKN (including PKN1) phosphorylates KRT8 (keratin 8) at Ser43, which impedes RAB33B trafficking from the Golgi, suppresses autophagosome initiation, and contributes to intervertebral disc degeneration; knockdown of Pkn1 and Pkn2 together ameliorates disc degeneration. |
Conditional Krt8 knockout, PKN1/2 knockdown, phospho-Ser43 KRT8 detection, RAB33B trafficking assay, autophagy initiation assay, in vivo disc degeneration models |
Autophagy |
High |
36897022
|
| 2006 |
The very C-terminus of PRK1/PKN1 (beyond the hydrophobic motif) is essential for activation by RhoA and for downstream signaling (neurite retraction); deletion of HR1 alone does not fully abolish RhoA binding or activation, indicating both the HR1 domain and C-terminus contribute to full RhoA-mediated activation. |
C-terminal deletion mutants, in vitro kinase activation assay with GTPγS-RhoA, in vivo RhoA activation assay, neurite retraction assay in neuronal cells |
Cellular signalling |
Medium |
16427251
|
| 1999 |
Drosophila Pkn (PKN ortholog) binds specifically to GTP-activated Rho1 and Rac1 through distinct binding sites, and both interactions increase kinase activity; genetic loss-of-function shows Pkn is required for epidermal cell shape changes during dorsal closure, acting in a Rho1-mediated pathway independent of the Rac-JNK pathway. |
Yeast two-hybrid, in vitro binding, in vitro kinase assay, Drosophila loss-of-function mutant, epistasis analysis |
Genes & development |
High |
10323867
|
| 2000 |
PKN1 binds and phosphorylates high-risk HPV E6 oncoprotein; only high-risk (not low-risk) HPV E6 proteins bind PKN1; this is the first demonstration that HPV E6 is a phosphoprotein. |
Yeast two-hybrid, in vitro binding (wheat-germ lysate), co-immunoprecipitation in 293T cells, in vitro kinase assay |
The Journal of biological chemistry |
Medium |
10809724
|
| 2000 |
PKN (PRK1/PKN1) stimulates transcriptional activity of the ANF promoter via the serum response element (SRE) in cardiomyocytes; only PKN (not PRK2 or Rho kinase) generates robust ANF-SRE stimulation; this effect requires RhoA and is lost with SRE mutation. |
Luciferase reporter assays, constitutively active PKN1 transfection, dominant-negative Rho, SRE mutagenesis |
American journal of physiology. Heart and circulatory physiology |
Medium |
10843871
|
| 2005 |
In PTEN-null MEFs, cortical actin formation is mediated through the PTEN/RhoA/PKN pathway, as dominant-negative RhoA or kinase-dead PKN inhibit cortical actin accumulation; however, this pathway does not mediate enhanced cell migration (which depends on Rac/PDK-1/Akt instead). |
Dominant-negative RhoA and kinase-dead PKN overexpression in Pten−/− MEFs, actin staining, cell migration assay |
Oncogene |
Medium |
15531926
|
| 2010 |
Hypotonic stress activates PKN1 via Thr774 phosphorylation in cardiac myocytes, with activation dependent on upstream PDK1 and Src-family kinase-mediated RhoA activation; active PKN1 promotes ERK phosphorylation via MEK to enhance cardiac myocyte survival. |
In vitro PKN1 activity assay, immunoblot for Thr774 phosphorylation, pharmacological inhibition (PP1, U-0126), Elk1-GAL4 transcriptional assay, siRNA knockdown, cell viability assay |
American journal of physiology. Heart and circulatory physiology |
Medium |
21037231
|
| 2023 |
Downstream of Gαq-RhoA in uveal melanoma, PKN converges with ROCK to control FAK signaling; darovasertib inhibits both PKC and PKN/PRK kinases and synergizes with FAK inhibitors in vitro and in preclinical metastatic models. |
High-throughput chemogenetic drug screen, kinase inhibitor profiling, FAK phosphorylation assay, in vitro cell viability assay, preclinical mouse metastasis model |
Cell reports. Medicine |
Medium |
37858338
|
| 2021 |
PKN1 negatively regulates hippocampal AKT activity and NeuroD2 levels; Pkn1 knockout elevates phospho-AKT and NeuroD2, leading to enhanced GluA1 (but not GluA2/3) protein levels and increased GluA1 membrane fraction, revealing a PKN1–AKT–NeuroD2–GluA1 regulatory axis. |
Pkn1 knockout mouse, immunoblot for phospho-AKT and NeuroD2, subcellular fractionation, flow cytometry for membrane GluA1 |
Frontiers in synaptic neuroscience |
Medium |
33613259
|
| 2023 |
PKN1 inhibition reduces AKT phosphorylation; PKN1 phosphorylation at S374 is functionally relevant for PKN1–AKT interaction and axonal outgrowth on inhibitory substrates in cerebellar granule cells; PKN1 pS374 decreases during cerebellar development. |
Pkn1 knockout cerebellar granule cells, hypoxia-ischemia in vitro model, AKT phosphorylation assay, axonal outgrowth assay, caspase-3 activation assay, site-specific mutagenesis of S374 |
Biomolecules |
Medium |
38002281
|
| 2026 |
PKN1 HR1a forms a dimer, and HR1c drives further oligomerization; RhoA forms a 1:2 complex with HR1a and induces rearrangement of the HR1a dimer (supported by SAXS), whereas Rac1 binds monomeric HR1a, suggesting distinct activation mechanisms for RhoA vs. Rac1. |
Biophysical analysis (SEC, AUC), SAXS, integrative structural modeling of HR1-containing PKN1 dimers |
The Journal of biological chemistry |
High |
42036044
|
| 2026 |
TDP-43 loss induces inclusion of a cryptic exon (PKN1-5a1) in PKN1 mRNA, generating a truncated peptide (PKN207) that escapes nonsense-mediated decay, is detectable in AD brains with TDP-43 pathology, and impairs cognition, memory, and synaptic plasticity in mice. |
RNA sequencing in ALS patient brains, NMD inhibition assay, mass spectrometry detection of PKN207 in AD brain, in vivo mouse cognitive/synaptic plasticity assays |
Nature communications |
Medium |
41720774
|
| 1998 |
PKN1 regulates alphaB-crystallin expression under heat stress via cooperation with HSF1; the catalytically active fragment of PKN1, but not the inactive form, induces alphaB-crystallin accumulation in HeLa cells through both proximal and distal heat shock elements of the promoter. |
Transfection of active/inactive PKN1 fragment with HSF1, luciferase reporter assay, alphaB-crystallin immunoblot |
Biochemical and biophysical research communications |
Medium |
9837746
|
| 1998 |
PKN1 interacts with the paraneoplastic cerebellar degeneration antigen PCD17 via its N-terminal regulatory domain; PKN1 phosphorylates PCD17 in a fatty acid-stimulated manner; PCD17 functions as a transcriptional activator and is co-immunoprecipitated with PKN1. |
Yeast two-hybrid, in vitro binding, co-immunoprecipitation from COS7 cells, in vitro kinase assay, transcriptional reporter assay |
Experimental cell research |
Medium |
9637778
|
| 1999 |
PKN1 interacts directly with the bHLH domain of the transcription factor NDRF/NeuroD2; co-expression of catalytically active PKN1 (but not kinase-deficient PKN1) further enhances NDRF/NeuroD2-dependent transcription of the insulin promoter element RIPE3. |
Yeast two-hybrid, in vitro binding with deletion mutants, co-immunoprecipitation from COS-7 cells, transient transfection reporter assay |
Brain research. Molecular brain research |
Medium |
10640683
|
| 2006 |
PKNα (PKN1) interacts with Cyclin T2a in a yeast two-hybrid screen and co-immunoprecipitation; co-overexpression of PKNα and Cyclin T2a strongly enhances expression of myogenic differentiation markers (Myogenin, Myosin Heavy Chain) in C2C12 cells during starvation-induced differentiation. |
Yeast two-hybrid, co-immunoprecipitation, in vitro pull-down, luciferase reporter assay, myogenic differentiation marker immunoblot |
Journal of cellular physiology |
Medium |
16331689
|
| 2024 |
The C2-like domain of PKN1 contains amphipathic cardiolipin-binding motifs and binds cardiolipin and C18 fatty acids; two distinct types of cardiolipin/phosphatidic acid binding are observed; the pseudosubstrate sequence in the C2 domain overlaps with the arachidonic acid binding region, linking lipid binding to autoinhibitory regulation. |
Biophysical lipid-binding assays (SPR/ITC), CD spectroscopy, sequence analysis, kinetic assay of full-length PKN1 |
Biochemistry |
Medium |
38441874
|
| 2007 |
Constitutively active PKN1 in mammary epithelium impairs tight junction sealing at parturition without disrupting tight junction formation (occludin and ZO1 localize correctly); dominant-negative PKN1 accelerates tight junction sealing in EpH4 cells, and active PKN1 impairs glucocorticoid-stimulated sealing. |
Transgenic mouse (mammary-specific CA-PKN1), intraductal [14C]sucrose injection for sealing assay, occludin/ZO1 immunofluorescence, EpH4 cell dominant-negative/active transfection |
Journal of cell science |
Medium |
17591691
|
| 2023 |
PKN1 controls adipocyte differentiation and glucose metabolism; PKN1-silenced adipocytes show decreased differentiation and glucose uptake with reduced PPARγ, FABP4, adiponectin, and CEBPα expression; insulin-resistant adipocytes show decreased PKN1 activation. |
siRNA knockdown in 3T3-L1 adipocytes and human VAT explants, glucose uptake assay, adipogenic marker immunoblot, PKN1 phosphorylation assay |
Nutrients |
Medium |
37242297
|
| 2019 |
PKN1 kinase activity is required for protection of TRAF1 from cIAP-mediated degradation during constitutive CD40 signaling; the active phospho-Thr774 form of PKN1 is constitutively expressed in CLL but not in healthy B cells. |
PKN1 kinase inhibitor treatment (OTSSP167, XL-228), TRAF1 immunoblot, caspase-3 activation assay in primary CLL samples |
Oncoimmunology |
Medium |
34589290
|
| 2025 |
Na+ and K+ ions directly and rapidly reduce PKN activation-loop phosphorylation in the absence of membranes; upon reduction of ion concentration, phosphorylation recovers without requiring PDK1 or ATP, via a 'reacquisition of phosphate' mechanism demonstrated by 32P tracing. |
Cell-free lysate PKN activation-loop phosphorylation assay with defined ion concentrations, PDK1-depleted lysate, 32P tracing experiment |
bioRxivpreprint |
Low |
bio_10.1101_2025.09.04.674365
|