Palmitoylation is required for Sept8-204 and Sept5 to form vesicle-like structure and colocalize with synaptophysin

J Cell Biochem. 2024 Mar;125(3):e30529. doi: 10.1002/jcb.30529. Epub 2024 Feb 3.

Abstract

Sept8 is a vesicle associated protein and there are two typical transcriptional variants (Sept8-204 and Sept8-201) expressed in mice brain. Interestingly, the coexpression of Sept8-204/Sept5 induces the formation of small sized vesicle-like structure, while that of the Sept8-201/Sept5 produces large puncta. Sept8 is previously shown to be palmitoylated. Here it was further revealed that protein palmitoylation is required for Sept8-204/Sept5 to maintain small sized vesicle-like structure and colocalize with synaptophysin, since either the expression of nonpalmitoylated Sept8-204 mutant (Sept8-204-3CA) or inhibiting Sept8-204 palmitoylation by 2-BP with Sept5 produces large puncta, which barely colocalizes with synaptophysin (SYP). Moreover, it was shown that the dynamic palmitoylation of Sept8-204 is controlled by ZDHHC17 and PPT1, loss of ZDHHC17 decreases Sept8-204 palmitoylation and induces large puncta, while loss of PPT1 increases Sept8-204 palmitoylation and induces small sized vesicle-like structure. Together, these findings suggest that palmitoylation is essential for the maintenance of the small sized vesicle-like structure for Sept8-204/Sept5, and may hint their important roles in synaptic functions.

Keywords: Sept8-204; dynamics; palmitoylation; puncta; vesicle-like structure.

MeSH terms

  • Animals
  • Cell Cycle Proteins / metabolism
  • Lipoylation*
  • Mice
  • Septins* / genetics
  • Septins* / metabolism
  • Synaptophysin / genetics
  • Synaptophysin / metabolism

Substances

  • Cell Cycle Proteins
  • Septins
  • Synaptophysin
  • Syp protein, mouse