Arabidopsis inositol polyphosphate kinases IPK1 and ITPK1 modulate crosstalk between SA-dependent immunity and phosphate-starvation responses

Author(s):  
Hitika Gulabani ◽  
Krishnendu Goswami ◽  
Yashika Walia ◽  
Abhisha Roy ◽  
Jewel Jameeta Noor ◽  
...  
2021 ◽  
Author(s):  
Hitika Gulabani ◽  
Krishnendu Goswami ◽  
Yashika Walia ◽  
Jewel Jameeta Noor ◽  
Kishor D. Ingole ◽  
...  

AbstractThe propensity for polyphosphorylation makes myo-inositol derivatives, the inositol polyphosphates (InsPs), especially phytic acid or inositol hexakisphosphate (InsP6) the major form of phosphate storage in plants. Acts of pyrophosphorylation on InsP6 generates InsP7 or InsP8 containing high-energy phosphoanhydride bonds that are harnessed during energy requirements of a cell. Also implicated as co-factors for several phytohormone signaling networks, InsP7/InsP8 modulate key developmental processes. With recent identification as the common moeity for transducing both jasmonic acid (JA) and phosphate-starvation responses (PSR), InsP8 is the classic example of a metabolite that may moonlight crosstalks to different cellular pathways during diverse stress adaptations. We show here that Arabidopsis thaliana INOSITOL PENTAKISPHOSPHATE 2-KINASE (IPK1), INOSITOL 1,3,4-TRISPHOSPHATE 5/6-KINASE 1 (ITPK1), and DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE 2 (VIH2), but not other InsP-kinases, suppress basal salicylic acid (SA)-dependent immunity. In ipk1, itpk1 or vih2 mutants, elevated endogenous SA levels and constitutive activation of defense signaling lead to enhanced resistance against the virulent Pseudomonas syringae pv tomato DC3000 (PstDC3000) strain. Our data reveal that activated SA-signaling sectors in these mutants modulate expression amplitudes of phosphate-starvation inducible (PSI)-genes, reported earlier. In turn, via mutualism the heightened basal defenses in these mutants require upregulated PSI-gene expressions likely highlighting the increased demand of phosphates required to support immunity. We demonstrate that SA is induced in phosphate-deprived plants, however its defense-promoting functions are likely diverted to PSR-supportive roles. Overall, our investigations reveal selective InsPs as crosstalk mediators among diverse signaling networks programming stress-appropriate adaptations.


2020 ◽  
Author(s):  
Yashika Walia ◽  
Kishor D Ingole ◽  
Mritunjay Kasera ◽  
Swaroop Peddiraju ◽  
Debabrata Laha ◽  
...  

AbstractTargeted protein degradation is essential for physiological development and adaptation to stress. Mammalian INOSITOL PENTAKISPHOSPHATE KINASE (IP5K) and INOSITOL HEXAKISPHOSPHATE KINASE 1 (IP6K1) pair modulates functions of Cullin RING Ubiquitin E3 ligases (CRLs) that execute targeted degradation of substrates. Coordinated activities of these kinases protect CRLs on a COP9 signalosome (CSN) platform and stimulates deneddylation-dependent disassembly to maintain continuity of its functions. In plants, CRL regulations on CSN by inositol phosphate (InsP) kinases are not known. Here, we show interactions of Arabidopsis thaliana INOSITOL PENTAKISPHOSPHATE 2-KINASE 1 (IPK1) and INOSITOL 1,3,4-TRISPHOSPHATE 5/6-KINASE 1 (ITPK1), counterparts of the above InsP-kinase pair, with CSN subunits and its positive influences on the dynamics of cullin deneddylation. We identify neddylation enhancements on CRLs as an early response to phosphate-starvation and its orchestration by perturbed IPK1/ITPK1 activities. At a molecular level, specific kinetics of CSN5 deneddylase is affected by the above InsP-kinases. Overall, our data reveal conserved InsP-kinase involvements on CRL-CSN synergism in plants.


Sign in / Sign up

Export Citation Format

Share Document