Protein palmitoylation increases the protein hydrophobicity by lipid modification in cancer cells, facilitating the proteins’ propensity to anchor to any membrane. To date, the palmitoylome has been mainly described in the cytosol and the Golgi apparatus. INCENP is a nucleoprotein, which plays a critical role at the centromere in ensuring strict chromosome alignment and segregation during mitosis (Klein et al., 2006; Becker et al., 2010). The reversible S-palmitoylation of INCENP may not only take place in the cytoplasm but may also occur in the nucleus. We unexpectedly discovered that ZDHHC5, ZDHHC14, ZDHHC16, and ZDHHC23 were located in the cell nucleus in our analysis. This localization may facilitate the propensity of INCENP proteins to anchor to nuclear membranes and reach the nucleus; although, we may consider its nuclear location as a potential prerequisite for nucleoprotein palmitoylation within the nucleus. Thus, although the evaluation of the direct interaction between ZDHHC5 and INCENP was not sufficiently performed in this study, its nuclear localization and the presence of the S-palmitoylation site appear to be essential for timely, complete, and efficient S-palmitoylation to occur.
