scholarly journals Comprehensive Phosphoproteomic Analysis of Pepper Fruit Development Provides Insight into Plant Signaling Transduction

2020 ◽  
Vol 21 (6) ◽  
pp. 1962 ◽  
Author(s):  
Zhoubin Liu ◽  
Junheng Lv ◽  
Yuhua Liu ◽  
Jing Wang ◽  
Zhuqing Zhang ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Fruit Development ◽  
Development Stage ◽  
Receptor Protein ◽  
Plant Signaling ◽  
Signaling Transduction ◽  
Calcium Dependent ◽  
Pepper Fruit ◽  
Mitogen Activated Protein ◽  
Dependent Protein

Limited knowledge is available for phosphorylation modifications in pepper (Capsicum annuum L.), especially in pepper fruit development. In this study, we conducted the first comprehensive phosphoproteomic analysis of pepper fruit at four development stage by Tandem Mass Tag proteomic approaches. A total of 2639 unique phosphopeptides spanning 1566 proteins with 4150 nonredundant sites of phosphorylation were identified, among which 2327 peptides in 1413 proteins were accurately quantified at four different stages. Mature Green (MG) to breaker stage showed the largest number of differentially expressed phosphoproteins and the number of downregulated phosphoproteins was significantly higher than that of upregulated after MG stage. Twenty seven phosphorylation motifs, including 22 pSer motifs and five pThr motifs and 85 kinase including 28 serine/threonine kinases, 14 receptor protein kinases, six mitogen-activated protein kinases, seven calcium-dependent protein kinases, two casein kinases, and some other kinases were quantified. Then the dynamic changes of phosphorylated proteins in ethylene and abscisic acid signaling transduction pathways during fruit development were analyzed. Our results provide a cascade of phosphoproteins and a regulatory network of phosphorylation signals, which help to further understand the mechanism of phosphorylation in pepper fruit development.

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.

Calcium-Dependent Protein Kinases (CDPK) in Abiotic Stress Tolerance

2018 ◽  
Vol 34 (2) ◽  
pp. 259-265 ◽  
Author(s):  
Hemant B Kardile ◽  
◽  
Vikrant ◽  
Nirmal Kant Sharma ◽  
Ankita Sharma ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Stress Tolerance ◽  
Protein Kinases ◽  
Abiotic Stress Tolerance ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinases

scholarly journals Extracellular matrix and integrin signalling: the shape of things to come

1999 ◽  
Vol 339 (3) ◽  
pp. 481-488 ◽  
Author(s):  
Nancy J. BOUDREAU ◽  
Peter Lloyd JONES
Keyword(s):  
Extracellular Matrix ◽  
Protein Kinases ◽  
Cell Shape ◽  
Large Body ◽  
Three Dimensional ◽  
Small Gtpases ◽  
Intracellular Signalling ◽  
Receptor Protein ◽  
Stringent Requirement ◽  
Mitogen Activated Protein

The extracellular matrix (ECM) and integrins collaborate to regulate gene expression associated with cell growth, differentiation and survival. Biochemical and molecular analyses of integrin signalling pathways have uncovered several critical cytoplasmic proteins that link the ECM and integrins to intracellular pathways that may contribute to anchorage-dependent growth. A large body of evidence now indicates that the non-receptor protein kinases focal adhesion kinase (FAK) and specific members of the mitogen-activated protein kinases (MAPKs), including the extracellular-signal-regulated kinases (ERKs), mediate these ECM- and integrin-derived signalling events. However, little is known about how FAK and MAPKs contribute to biological processes other than cell proliferation or migration. In addition, remarkably little is known concerning the signalling events that occur in cells that adhere to complex multivalent extracellular matrices via multiple integrin receptors. Given the stringent requirement for attaining a proper morphology in ECM/integrin-directed cell behaviour, it is still not clear how cell shape and tissue architecture impact upon intracellular signalling programmes involving FAK and MAPKs. However, the recent discovery that members of the Rho family of small GTPases are able to regulate ECM/integrin pathways that modulate both cell shape and intracellular signalling provides new insights into how cell morphology and signal transduction become integrated, especially within three-dimensional differentiated tissues.

Sign in / Sign up

Export Citation Format

Share Document