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Cell division requires dramatic reorganization of the cell cortex which is primarily driven by the actomyosin network. We previously reported that Protocadherin 7 (PCDH7) gets enriched at the cell surface during mitosis which is required to build up the full mitotic rounding pressure. Here we report that PCDH7 interacts with, and is palmitoylated by the palmitoyltransferase, ZDHHC5. Both PCDH7 and ZDHHC5 co-localize at the mitotic cell surface, and translocate to the cleavage furrow during cytokinesis. PCDH7's localization depends on the palmitoylation activity of ZDHHC5. Silencing PCDH7 increases the percentage of multinucleated cells and the duration of mitosis. Loss of PCDH7 expression correlates with reduced levels of active RhoA and phospho-myosin at the cleavage furrow. This work uncovers a palmitoylation-dependent translocation mechanism for PCDH7 which contributes to the reorganization of the cortical cytoskeleton during cell division.

Successful cell division requires dramatic reorganization of the cell cortex in coordination with actomyosin cytoskeleton organization, membrane trafficking and cell adhesion. Although the contractile actomyosin ring is considered as hallmark of cytokinesis, in some cell types cell adhesion systems have been shown to drive cytokinesis independently from actomyosin function. We previously reported that Protocadherin 7 (PCDH7) localizes to the mitotic cortex which is required for building up the full mitotic rounding pressure. Here, we show that PCDH7 localizes to the mitotic cell cortex and to the cleavage furrow by a palmitoylation-dependent mechanism. At the cleavage furrow, PCDH7 facilitates the activation of myosin II and successful cytokinesis. Strikingly, PCDH7 promotes cytokinesis even when the myosin II contractility and integrin mediated adhesion are blocked. This work describes a palmitoylation-dependent cortical reorganization which promotes cytokinesis under different conditions.