Two amino acid sequences direct Aspergillus nidulans protein kinase C (PkcA) localization to hyphal apices and septation sites

Mycologia ◽  
2015 ◽  
Vol 107 (3) ◽  
pp. 452-459 ◽  
Author(s):  
Loretta Jackson-Hayes ◽  
Terry W. Hill ◽  
Darlene M. Loprete ◽  
Claire E. DelBove ◽  
Justin A. Shapiro ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Aspergillus Nidulans ◽  
Amino Acid Sequences ◽  
Kinase C

scholarly journals Amino acid sequence and characterization of a protein inhibitor of protein kinase C.

1990 ◽  
Vol 265 (8) ◽  
pp. 4583-4591 ◽  
Author(s):  
J D Pearson ◽  
D B DeWald ◽  
W R Mathews ◽  
N M Mozier ◽  
H A Zürcher-Neely ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Protein Inhibitor ◽  
Kinase C

Activators of protein kinase A and of protein kinase C inhibit MDCK cell myo-inositol and betaine uptake.

1995 ◽  
Vol 6 (6) ◽  
pp. 1559-1564
Author(s):  
A S Preston ◽  
A Yamauchi ◽  
H M Kwon ◽  
J S Handler
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Translational Regulation ◽  
Mdck Cells ◽  
Relative Effect ◽  
Amino Acid Sequences ◽  
Prolonged Incubation ◽  
Kinase C ◽  
Kinase A

Amino acid sequences of the myo-inositol and betaine cotransporters that are induced in MDCK cells by hypertonicity include consensus sequences for phosphorylation by protein kinase A and by protein kinase C. To test for the effect of activation of protein kinases A and C on the activity of those cotransporters, MDCK cells were exposed to activators of each kinase and the activity of both cotransporters was assayed. Incubation with 8-bromoadenosine 3':5'-cyclic monophosphate (8Br-cAMP) or 3-isobutyl-1-methylxanthine (IBMX), activators of protein kinase A, and incubation with an active phorbol ester or with an active diacylglycerol, activators of protein kinase C, inhibited the activity of both cotransporters by about 30%. The relative effect of the activation of protein kinase A and of protein kinase C was similar in hypertonic and isotonic cells. The effects of activators of protein kinase A and of protein kinase C were not additive. The two cotransporters behaved differently when protein kinase C activity was down-regulated by prolonged incubation with a higher concentration of phorbol 12-myristate 13-acetate. There was a doubling of activity of the myo-inositol cotransporter and no change in the activity of the betaine cotransporter in hypertonic and isotonic cells. Although the mechanisms of the effects of activation of the two kinases remain to be established, it is clear that the kinases can mediate post-translational regulation of the uptake of compatible osmolytes.

Investigating the Protein Kinase C Polarized Growth‐Related Protein Complex in Aspergillus nidulans

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Loretta Jackson-Hayes ◽  
Alexis Craft ◽  
Muhammad Hameed ◽  
Zariah Hines ◽  
W. Toler Freyaldenhoven ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Aspergillus Nidulans ◽  
Protein Complex ◽  
Polarized Growth ◽  
Related Protein ◽  
Kinase C

Protein kinase C restricts transport of carnitine by amino acid transporter ATB0,+ apically localized in the blood–brain barrier

2014 ◽  
Vol 554 ◽  
pp. 28-35 ◽  
Author(s):  
Katarzyna Michalec ◽  
Caroline Mysiorek ◽  
Mélanie Kuntz ◽  
Vincent Bérézowski ◽  
Andrzej A. Szczepankiewicz ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Blood Brain Barrier ◽  
Amino Acid Transporter ◽  
Brain Barrier ◽  
Kinase C ◽  
Blood Brain ◽  
Acid Transporter

scholarly journals The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway.

1996 ◽  
Vol 16 (12) ◽  
pp. 6752-6764 ◽  
Author(s):  
T Toda ◽  
S Dhut ◽  
G Superti-Furga ◽  
Y Gotoh ◽  
E Nishida ◽  
...  
Keyword(s):  
Cell Wall ◽  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Fission Yeast ◽  
Mitogen Activated Protein Kinase ◽  
Cell Integrity ◽  
Kinase C ◽  
Mitogen Activated Protein ◽  
Mapk Gene

We have isolated a gene, pmk1+, a third mitogen-activated protein kinase (MAPK) gene homolog from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequence shows the most homology (63 to 65% identity) to those of budding yeast Saccharomyces Mpk1 and Candida Mkc1. The Pmk1 protein contains phosphorylated tyrosines, and the level of tyrosine phosphorylation was increased in the dsp1 mutant which lacks an attenuating phosphatase for Pmk1. The level of tyrosine phosphorylation appears constant during hypotonic or heat shock treatment. The cells with pmk1 deleted (delta pmk1) are viable but show various defective phenotypes, including cell wall weakness, abnormal cell shape, a cytokinesis defect, and altered sensitivities to cations, such as hypersensitivity to potassium and resistance to sodium. Consistent with a high degree of conservation of amino acid sequence, multicopy plasmids containing the MPK1 gene rescued the defective phenotypes of the delta pmk1 mutant. The frog MAPK gene also suppressed the pmk1 disruptant. The results of genetic analysis indicated that Pmk1 lies on a novel MAPK pathway which does not overlap functionally with the other two MAPK pathways, the Spk1-dependent mating signal pathway and Sty1/Spc1/Phh1-dependent stress-sensing pathway. In Saccharomyces cerevisiae, Mpk1 is involved in cell wall integrity and functions downstream of the protein kinase C homolog. In contrast, in S. pombe, Pmk1 may not act in a linear manner with respect to fission yeast protein kinase C homologs. Interestingly, however, these two pathways are not independent; instead, they regulate cell integrity in a coordinate manner.

Sign in / Sign up

Export Citation Format

Share Document