{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,4]],"date-time":"2026-02-04T04:49:28Z","timestamp":1770180568146,"version":"3.49.0"},"reference-count":20,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T00:00:00Z","timestamp":1764633600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,2,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Phospholipase A (PLA) and acyltransferases coordinate glycerophospholipid remodeling to maintain membrane diversity and function. The phospholipase A and acyltransferase (PLAAT) family combines PLA1\/PLA2 with N- and O-acyltransferase activities, generating N-acylethanolamines with diverse bioactivities and enabling acyl-CoA-independent remodeling. PLAAT3 has been identified as a causative gene for human lipodystrophy. In addition to adipocyte dysfunction, PLAAT3-deficient mice develop cataracts due to impaired organelle degradation in lens fiber cells. In non-mammalian vertebrates such as zebrafish, which lack PLAAT3, PLAAT1 is highly expressed in the lens, and its deficiency similarly causes cataract-like abnormalities by blocking organelle clearance. A recent study reported that PLAAT1 promotes cardiolipin production in cultured cells, indicating a role in mitochondrial membrane lipid metabolism; however, its direct involvement in mitochondrial dynamics remains unclear. To address this, Sikder et\u00a0al. (PLAAT1 expression triggers fragmentation of mitochondria in an enzyme activity-dependent manner. J Biochem 2023;175:101\u201313) established a doxycycline-inducible mouse PLAAT1 expression system in HEK293 cells. Catalytically active PLAAT1 rapidly induced mitochondrial fragmentation and peroxisome loss, independently of changes in Drp1, Mfn2 and Opa1 expression. These findings reveal a previously unrecognized role of PLAAT1 in regulating organelle dynamics and maintaining cellular homeostasis.<\/jats:p>","DOI":"10.1093\/jb\/mvaf076","type":"journal-article","created":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T09:46:21Z","timestamp":1764668781000},"page":"83-86","source":"Crossref","is-referenced-by-count":0,"title":["Phospholipase A and acyltransferases as novel regulator of organelle dynamics"],"prefix":"10.1093","volume":"179","author":[{"given":"Naoki","family":"Matsumoto","sequence":"first","affiliation":[{"name":"Faculty of Pharmaceutical Sciences, Teikyo University , 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2544-2134","authenticated-orcid":false,"given":"Atsushi","family":"Yamashita","sequence":"additional","affiliation":[{"name":"Faculty of Pharmaceutical Sciences, Teikyo University , 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2025,12,2]]},"reference":[{"key":"2026020310571750100_ref1","first-page":"23","article-title":"Coenzyme-A-independent transacylation system: possible involvement of phospholipase A2 in transacylation","volume":"6","author":"Yamashita","year":"2017","journal-title":"Biology (Basel)"},{"key":"2026020310571750100_ref2","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.bbalip.2017.08.006","article-title":"Mammalian enzymes responsible for the biosynthesis of N-acylethanolamines","volume":"1862","author":"Hussain","year":"2017","journal-title":"Biochim. 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