Differential Phosphorylation of Human Tau Isoforms Containing Three Repeats by Several Protein Kinases

1996 ◽  
Vol 328 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Toolsee J. Singh ◽  
Inge Grundke-Iqbal ◽  
Khalid Iqbal
Keyword(s):  
Protein Kinases ◽  
Tau Isoforms ◽  
Differential Phosphorylation

scholarly journals Differential phosphorylation of ribosomal acidic proteins from yeast cell by two endogenous protein kinases: casein kinase-2 and 60S kinase.

1995 ◽  
Vol 42 (3) ◽  
pp. 357-362 ◽  
Author(s):  
R Szyszka ◽  
A Boguszewska ◽  
N Grankowski ◽  
J P Ballesta
Keyword(s):  
Protein Kinases ◽  
Ribosomal Subunit ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Amino Acid Sequences ◽  
The Other ◽  
Endogenous Protein ◽  
Target Amino Acid ◽  
Acidic Proteins ◽  
Differential Phosphorylation

The native 80S ribosomes isolated from Saccharomyces cerevisiae (strain W303) cells was phosphorylated by two endogenous protein kinases: multifunctional casein kinase-2 (CK-2) and specific 60S kinase. Three acidic proteins within the 60S ribosomal subunit: YP1 beta, YP1 beta' and YP2 alpha are phosphorylated by both kinases. The other two proteins: YP1 alpha and YP2 beta are predominantly phosphorylated by CK-2 but not by 60S kinase. This was confirmed in the experiment with the recombinant protein, YP2 beta, as a substrate, which is practically not phosphorylated by specific 60S kinase. These results together with the previous data based on the target amino-acid sequences suggest that, in addition to the multifunctional casein kinase-2 and specific 60S kinase, there exist probably other protein kinase(s) which phosphorylate the ribosomal acidic proteins in the cell.

scholarly journals Differential Phosphorylation of the Transcription Factor WRKY33 by the Protein Kinases CPK5/CPK6 and MPK3/MPK6 Cooperatively Regulates Camalexin Biosynthesis in Arabidopsis

2020 ◽  
Vol 32 (8) ◽  
pp. 2621-2638 ◽  
Author(s):  
Jinggeng Zhou ◽  
Xiaoyang Wang ◽  
Yunxia He ◽  
Tian Sang ◽  
Pengcheng Wang ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Protein Kinases ◽  
Differential Phosphorylation

Phosphoproteomic Profiling Reveals the Importance of CK2, MAPKs and CDPKs in Response to Phosphate Starvation in Rice

2019 ◽  
Vol 60 (12) ◽  
pp. 2785-2796 ◽  
Author(s):  
Jian Yang ◽  
Meng-Yang Xie ◽  
Xiao-Li Yang ◽  
Bao-Hui Liu ◽  
Hong-Hui Lin
Keyword(s):  
Protein Kinases ◽  
Sufficient Conditions ◽  
Motif Analysis ◽  
Calcium Dependent ◽  
Phosphorylated Proteins ◽  
Pi Starvation ◽  
Mitogen Activated Protein ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinases ◽  
Differential Phosphorylation

Abstract Phosphorus is one of the most important macronutrients required for plant growth and development. The importance of phosphorylation modification in regulating phosphate (Pi) homeostasis in plants is emerging. We performed phosphoproteomic profiling to characterize proteins whose degree of phosphorylation is altered in response to Pi starvation in rice root. A subset of 554 proteins, including 546 down-phosphorylated and eight up-phosphorylated proteins, exhibited differential phosphorylation in response to Pi starvation. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis with the differentially phosphorylated proteins indicated that RNA processing, transport, splicing and translation and carbon metabolism played critical roles in response to Pi starvation in rice. Levels of phosphorylation of four mitogen-activated protein kinases (MAPKs), including OsMAPK6, five calcium-dependent protein kinases (CDPKs) and OsCK2β3 decreased in response to Pi starvation. The decreased phosphorylation level of OsMAPK6 was confirmed by Western blotting. Mutation of OsMAPK6 led to Pi accumulation under Pi-sufficient conditions. Motif analysis indicated that the putative MAPK, casein kinase 2 (CK2) and CDPK substrates represented about 54.4%, 21.5% and 4.7%, respectively, of the proteins exhibiting differential phosphorylation. Based on the motif analysis, 191, 151 and 46 candidate substrates for MAPK, CK2 and CDPK were identified. These results indicate that modification of phosphorylation profiles provides complementary information on Pi-starvation-induced processes, with CK2, MAPK and CDPK protein kinase families playing key roles in these processes in rice.

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