Publications of NIPGR Scientists

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Author: search.filters.author.Singh, KirtiSubject: search.filters.subject.Arabidopsis thaliana

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    Mitogen-activated protein kinase 3/6 regulates the stability of AtIAA3 and AtIAA7 during auxin signaling in Arabidopsis
    (Elsevier B.V., 2026) Noryang, Stanzin; Manna, Mrinalini; Verma, Neetu; Singh, Kirti; Tayyeba, Sumaira; Sinha, Alok Krishna
    Auxin mediated Aux/IAA degradation is required to release the ARFs from the control of IAAs, and ARFs in the free forms perform their role of transcription activation or suppression in response to developmental ques. Auxin is known to tag IAAs for proteasomal degradation, but how this tagging is regulated has not been widely explored. Here we report that, in Arabidopsis, exogenous application of auxin activates MPK3/6 which in turn phosphorylate IAA3 and IAA7 at Ser-58 and Ser-26, respectively. Further, incubation of IAA3 and IAA7 with the protein extracts from auxin treated mpk3 or mpk6 single mutants increase the rate of degradation of IAAs. Consequently, the phospho-null mutants, IAA3S58A and IAA7S26A were observed to be comparatively more stable. Thus, MAP kinase-mediated phosphorylation destabilised IAA3 and IAA7 leading to their degradation. Additionally, over-expression of the phospho-dead mutant of IAA3 (35S:IAA3S58A) and complementation of iaa3 mutant with this phospho-dead mutant resulted in reduced primary root length because of increased stability and accumulation of IAA3. Interestingly, we found that a member of ARF, ARF7 regulated the expression of MPKs by binding to their respective promoters.
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    Dynamic phosphorylation of miRNA biogenesis factor HYL1 by MPK3 involving nuclear–cytoplasmic shuttling and protein stability in Arabidopsis
    (MDPI AG, 2022) Bhagat, Prakash Kumar; Verma, Deepanjali; Singh, Kirti; Badmi, Raghuram; Sharma, Deepika; Sinha, Alok Krishna
    MicroRNAs (miRNAs) are one of the prime regulators of gene expression. The recruitment of hyponastic leaves 1 (HYL1), a double-stranded RNA binding protein also termed as DRB1, to the microprocessor complex is crucial for accurate primary-miRNA (pri-miRNA) processing and the accumulation of mature miRNA in Arabidopsis thaliana. In the present study, we investigated the role of the MAP kinase-mediated phosphorylation of AtHYL1 and its sub-cellular activity. AtMPK3 specifically phosphorylates AtHYL1 at the evolutionarily conserved serine-42 present at the Nterminal regions and plays an important role in its nuclear–cytosolic shuttling. Additionally, we identified that AtHYL1 is cleaved by trypsin-like proteases into an N-terminal fragment, which renders its subcellular activities. We, for the first time, report that the dimerization of AtHYL1 not only takes place in the nucleus, but also in the cytosol, and the C-terminal of AtHYL1 has a role in regulating its stability, as well as its subcellular localization. AtHYL1 is hyper-phosphorylated in mpk3 mutants, leading to higher stability and reduced degradation. Our data show that AtMPK3 is a negative regulator of AtHYL1 protein stability and that the AtMPK3-induced phosphorylation of AtHYL1 leads to its protein degradation.