Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth and viability

PLoS One. 2019 Feb 8;14(2):e0198149. doi: 10.1371/journal.pone.0198149. eCollection 2019.


Palmitoylation is an important posttranslational modification regulating diverse cellular functions. Consequently, aberrant palmitoylation can lead to diseases such as neuronal disorders or cancer. In humans there are roughly one hundred times more palmitoylated proteins than enzymes catalyzing palmitoylation (palmitoyltransferases). Therefore, it is an important challenge to establish the links between palmitoyltransferases and their targets. From publicly available data, we find that expression of human ZDHHC8 correlates significantly with cancer survival. To elucidate the organismal function of ZDHHC8, we study the Drosophila ortholog of hZDHHC8, CG34449/dZDHHC8. Knockdown of dZDHHC8 causes tissue overgrowth while dZDHHC8 mutants are larval lethal. We provide a list of 159 palmitoylated proteins in Drosophila and present data suggesting that scribble and Ras64B are targets of dZDHHC8.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / genetics
  • Acyltransferases / metabolism*
  • Animals
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / growth & development
  • Humans
  • Lipoylation / physiology
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism
  • Neurons / metabolism
  • Protein Processing, Post-Translational
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / metabolism
  • ras Proteins / genetics
  • ras Proteins / metabolism*


  • Drosophila Proteins
  • Membrane Proteins
  • Ras64B protein, Drosophila
  • SCRIB protein, human
  • Scrib protein, Drosophila
  • Tumor Suppressor Proteins
  • Acyltransferases
  • ZDHHC8 protein, human
  • Metalloendopeptidases
  • YME1L protein, zebrafish
  • ras Proteins

Grant support

This work was partially funded by Helmholtz Postdoc Programm. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.