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To\u00a0elucidate the role of PATL1\u2010mediated vesicle trafficking in thermotolerance, we investigated PATL1 function under heat shock (HS) conditions and found PATL1 inhibited vesicle trafficking, leading to a decreased accumulation of HS proteins (HSPs), indicating a negative correlation with thermotolerance. Previously, we reported that the calmodulin (CaM) isoform, CaM3, is involved in heat tolerance. In the present study, we found that CaM3 binds to and inhibits PATL1, thereby promoting HSP accumulation. This interaction reduces the binding of PATL1 to phosphatidylinositol diphosphate, thereby facilitating vesicle transport. In\u00a0summary, our study elucidates a non\u2010canonical CaM3 signaling pathway in which PATL1 acts as a downstream factor to enhance HSP accumulation through vesicle trafficking.\n                  <\/jats:p>","DOI":"10.1111\/tpj.70865","type":"journal-article","created":{"date-parts":[[2026,4,19]],"date-time":"2026-04-19T11:30:32Z","timestamp":1776598232000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The\n                    <i>Arabidopsis thaliana<\/i>\n                    <scp>PATL1<\/scp>\n                    functions downstream of CaM3 to mediate vesicle trafficking under the heat shock pathway"],"prefix":"10.1111","volume":"126","author":[{"given":"Xinmiao","family":"Kang","sequence":"first","affiliation":[{"name":"Key Laboratory of Molecular and Cellular Biology of the Ministry of Education, Hebei Research Center of the Basic Discipline of Cell Biology, Hebei Collaboration Innovation Center for Cell 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