Protein kinase N controls a lysosomal lipid switch to facilitate nutrient signalling via mTORC1

2019 ◽  
Vol 21 (9) ◽  
pp. 1093-1101 ◽  
Author(s):  
Alexander Wallroth ◽  
Philipp A. Koch ◽  
Andrea L. Marat ◽  
Eberhard Krause ◽  
Volker Haucke
Keyword(s):  
Protein Kinase ◽  
Protein Kinase N

The Protein Kinase N (PKN) GenePRKCL1/Prkcl1Maps to Human Chromosome 19p12–p13.1 and Mouse Chromosome 8 with Close Linkage to the Myodystrophy (myd) Mutation

Genomics ◽  
1998 ◽  
Vol 49 (1) ◽  
pp. 129-132
Author(s):  
Jörg W. Bartsch ◽  
Hideyuki Mukai ◽  
Nobuaki Takahashi ◽  
Melanie Ronsiek ◽  
Sonja Fuchs ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Human Chromosome ◽  
Mouse Chromosome ◽  
Chromosome 8 ◽  
Close Linkage ◽  
Protein Kinase N ◽  
Mouse Chromosome 8

Protein kinase inhibitor H-89 reverses forskolin stimulation of cardiac L-type calcium current

1995 ◽  
Vol 268 (3) ◽  
pp. C651-C659 ◽  
Author(s):  
W. Yuan ◽  
D. M. Bers
Keyword(s):  
Protein Kinase ◽  
Patch Clamp ◽  
Kinase Inhibitor ◽  
Ventricular Myocytes ◽  
Calcium Currents ◽  
Maximal Conductance ◽  
Perforated Patch ◽  
Dependent Inactivation ◽  
Protein Kinase N ◽  
Steady State Inactivation

Calcium currents (ICa) and barium currents (IBa) were measured in freshly isolated single ferret ventricular myocytes, using the whole cell patch-clamp and perforated patch-clamp techniques with Na and K currents blocked by tetraethylammonium and Cs. The membrane potential (Em) dependence of activation and steady-state inactivation curves were determined using a Boltzmann relation, where E0.5 is the Em at half-maximal conductance. Forskolin (1 microM) increased the rate of ICa inactivation, especially in perforated patch, but slowed IBa inactivation. The acceleration is likely to be due to greater Ca-dependent inactivation of ICa, where the slowing of IBa inactivation may be due to protein kinase A-dependent slowing of Em-dependent inactivation. Forskolin (1-10 microM) also increased ICa amplitude by two- to threefold and shifted the E0.5 for both activation and inactivation to more negative potentials by 7-8 mV. The effect of forskolin on the amplitude of ICa could be reversed by an inhibitor of adenosine 3',5'-cyclic monophosphate-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89; 1-10 microM). However, H-89 did not reverse the shift of E0.5 induced by forskolin. H-89 application by itself does not decrease basal ICa but does shift the E0.5 of both activation and inactivation to more negative values of Em. It is possible that H-89 reverses the shift induced by regulatory phosphorylation (due to forskolin) but induces a coincidental negative shift itself.

scholarly journals Drosophila protein kinase N (Pkn) is a negative regulator of actin–myosin activity during oogenesis

2014 ◽  
Vol 394 (2) ◽  
pp. 277-291 ◽  
Author(s):  
Tânia Ferreira ◽  
Pedro Prudêncio ◽  
Rui Gonçalo Martinho
Keyword(s):  
Protein Kinase ◽  
Negative Regulator ◽  
Protein Kinase N ◽  
Drosophila Protein

Protein Kinase N (PKN) and PKN-Related Protein Rhophilin as Targets of Small GTPase Rho

Science ◽  
1996 ◽  
Vol 271 (5249) ◽  
pp. 645-648 ◽  
Author(s):  
G. Watanabe ◽  
Y. Saito ◽  
P. Madaule ◽  
T. Ishizaki ◽  
K. Fujisawa ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Small Gtpase ◽  
Related Protein ◽  
Protein Kinase N

Phosphorylation of RNA polymerases: specific association of protein kinase NIl with RNA polymerase I

1983 ◽  
Vol 302 (1108) ◽  
pp. 135-142 ◽  
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Synthesis ◽  
Rna Polymerase Iii ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Liver Protein ◽  
Protein Kinase N ◽  
Polymerase I

The activities of the three DNA-dependent RNA polymerases from a rapidly growing rat tumour, Morris hepatoma 3924 A, and from rat liver were examined. The activity of RNA polymerase I was higher in the tumour than in the liver. The enhanced capacity for RNA synthesis was a result of a higher concentration of polymerase I in the tumour as well as of an activation of this enzyme vivo. The possibility that the high specific activity of the hepatoma polymerase I resulted from phosphorylation was investigated. Two major cyclic-AMP-independent nuclear casein kinases (NI and N il) were identified; the activity of protein kinase N il in the tumour was ten times that in liver. Protein kinase N il was capable of activating and phosphorylating RNA polymerase I in vitro . This kinase could also stimulate RNA polymerase II activity, although to a lesser extent than RNA polymerase I. RNA polymerase III was not affected by protein kinase NIL Protein kinase N il was tightly associated with polymerase I and was found even in purified preparations of the polymerase. Antibodies against both RNA polymerase I and protein kinase N il were present in sera of patients with certain rheumatic autoimmune diseases. These results imply that RNA polymerase I and protein kinase NIl are in close association in vivo as well as in vitro and that polymerase phosphorylation may regulate the rate of ribosomal RNA synthesis in the cell.

scholarly journals Comparative Effects of GTPγS and Insulin on the Activation of Rho, Phosphatidylinositol 3-Kinase, and Protein Kinase N in Rat Adipocytes

1998 ◽  
Vol 273 (13) ◽  
pp. 7470-7477 ◽  
Author(s):  
Mary Standaert ◽  
Gautam Bandyopadhyay ◽  
Lamar Galloway ◽  
Yashitako Ono ◽  
Hideyuki Mukai ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Phosphatidylinositol 3 Kinase ◽  
Rat Adipocytes ◽  
Protein Kinase N ◽  
Phosphatidylinositol 3

Identification of a Putative Target for Rho as the Serine-Threonine Kinase Protein Kinase N

Science ◽  
1996 ◽  
Vol 271 (5249) ◽  
pp. 648-650 ◽  
Author(s):  
M. Amano ◽  
H. Mukai ◽  
Y. Ono ◽  
K. Chihara ◽  
T. Matsui ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Putative Target ◽  
Protein Kinase N

scholarly journals Axokinin phosphorylation by cAMP-dependent protein kinase is sufficient for activation of sperm flagellar motility.

1986 ◽  
Vol 103 (2) ◽  
pp. 649-655 ◽  
Author(s):  
J S Tash ◽  
H Hidaka ◽  
A R Means
Keyword(s):  
Protein Kinase ◽  
De Novo ◽  
Protein Kinase Activity ◽  
Dependent Manner ◽  
Flagellar Motility ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Heat Stable ◽  
Protein Kinase N ◽  
Dependent Protein

Using a selective inhibitor of cAMP-dependent protein kinase, N-[2(methylamino)ethyl]-5-isoquinolinesulfonamide (H-8), the requirement for cAMP-dependent phosphoproteins in the initiation of dog sperm flagellar motility was examined. H-8 inhibited motility of live as well as reactivated sperm in a dose-dependent manner. The half-maximal inhibition of reactivated motility (32 microM) paralleled the inhibition of pure catalytic subunit of cAMP-dependent protein kinase (50 microM) measured under the same conditions. H-8 inhibited protein phosphorylation both in whole models and in isolated Nonidet P-40 (NP-40) extracts of sperm. Axokinin, the heat-stable NP-40-soluble protein whose phosphorylation is required for flagellar reactivation, represented 97% of the de novo phosphate incorporation in the NP-40 extract after stimulation by cAMP. 500 microM H-8 inhibited axokinin phosphorylation by 87%. When sperm were reactivated in the presence of up to 5 mM H-8 with NP-40 extract that had been prephosphorylated with cAMP-dependent protein kinase, then neither cAMP nor cAMP-dependent protein kinase activity was required for full flagellar reactivation. If sperm were rendered completely immotile by pretreatment with H-8, then the resulting model remained immotile in the continued presence of H-8 unless prephosphorylated axokinin was added. These results suggest that phosphorylated axokinin is not only required for flagellar reactivation but is sufficient as well.

Sign in / Sign up

Export Citation Format

Share Document