In this study, greater periodontal breakdown, including probing depth, attachment loss, and radiographic alveolar bone loss, was found at the distal sites, but not at the mesial sites, of the experimental molars where the third molar was surgically extracted compared with the control teeth (no surgery). In the experimental molars, more radiographic bone loss was found at the sites adjacent to the surgical location than at the sites distant to the surgical location. Therefore, we suggest that the surgical removal of the mandibular third molar may lead to a periodontal breakdown on the distal surface of the second molar. Periodontal re-evaluation after the initial healing of third molar extraction is indicated.

Key Points PML selectively activates NLRP3 inflammasome. Targeting to PML could be used to attenuate NLRP3 inflammasome–associated pathogenesis.

Macroautophagy/autophagy is an important intracellular mechanism for the maintenance of cellular homeostasis. Here we show that the CERKL (ceramide kinase like) gene, a retinal degeneration (RD) pathogenic gene, plays a critical role in regulating autophagy by stabilizing SIRT1. In vitro and in vivo, suppressing CERKL results in impaired autophagy. SIRT1 is one of the main regulators of acetylation/deacetylation in autophagy. In CERKL-depleted retinas and cells, SIRT1 is downregulated. ATG5 and ATG7, 2 essential components of autophagy, show a higher degree of acetylation in CERKL-depleted cells. Overexpression of SIRT1 rescues autophagy in CERKL-depleted cells, whereas CERKL loses its function of regulating autophagy in SIRT1-depleted cells, and overexpression of CERKL upregulates SIRT1. Finally, we show that CERKL directly interacts with SIRT1, and may regulate its phosphorylation at Ser27 to stabilize SIRT1. These results show that CERKL is an important regulator of autophagy and it plays this role by stabilizing the deacetylase SIRT1.

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