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Inositol pyrophosphates (PP\u2010InsPs) are signaling molecules involved in P<jats:italic>i<\/jats:italic> sensing and jasmonic acid (JA)\u2010regulated plant defense. Here, we report that overexpression of 1,3,4\u2010trisphosphate 5\/6\u2010kinase 1 (ITPK1) and the kinase domain of the dual\u2010domain diphosphoinositol pentakisphosphate kinase 2 (VIP2KD) in <jats:italic>Arabidopsis thaliana<\/jats:italic> results in unique elevations in PP\u2010InsPs, accompanied by altered leaf growth and senescence patterns, as well as delayed time to flowering. While plants overexpressing ITPK1 and VIP2KD (ITPK1 OX and VIP2KD OX) accumulated significantly lower levels of P<jats:italic>i<\/jats:italic>, transcriptomic and qRT\u2010PCR analysis revealed that these plants showed elevated expression of P<jats:italic>i<\/jats:italic> starvation response genes. Our transcriptomic analysis also revealed ITPK1 OX and VIP2KD OX showed a significant enrichment in differentially expressed genes relating to plant defense and hypoxia. Of the two transgenic types, VIP2KD OX had significantly higher expression of more diverse plant defense\u2010related differentially expressed genes and showed greater resistance to <jats:italic>Trichoplusia ni<\/jats:italic> compared to WT and ITPK1 OX plants. ITPK1 OX, although also having elevated PP\u2010InsPs, was fed upon by insect larvae comparably to WT plants. Taken together, our data indicate the elevation of certain PP\u2010InsPs may be a useful strategy for developing new traits in crop plants.<\/jats:p>","DOI":"10.1111\/tpj.70315","type":"journal-article","created":{"date-parts":[[2025,7,10]],"date-time":"2025-07-10T23:14:54Z","timestamp":1752189294000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Enhancing inositol pyrophosphate accumulation in plants alters growth, phosphate homeostasis, and insect herbivory"],"prefix":"10.1111","volume":"123","author":[{"given":"Caitlin","family":"Cridland","sequence":"first","affiliation":[{"name":"Department of Biochemistry Virginia Tech  Blacksburg Virginia 24061 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashlynn","family":"Russo","sequence":"additional","affiliation":[{"name":"Department of Chemistry University of Richmond  Virginia 23173 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USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Glenda","family":"Gillaspy","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Wisconsin\u2010Madison  Wisconsin 53706 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9999-5930","authenticated-orcid":false,"given":"Catherine","family":"Freed","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Wisconsin\u2010Madison  Wisconsin 53706 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,7,10]]},"reference":[{"key":"e_1_2_9_2_1","article-title":"Inositol trisphosphate kinase and Diphosphoinositol Pentakisphosphate kinase enzymes constitute the inositol pyrophosphate synthesis pathway in plants","author":"Adepoju 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