International Journal of Cell Biology / 2012 / Article / Tab 1

Research Article

Antiproliferative Factor-Induced Changes in Phosphorylation and Palmitoylation of Cytoskeleton-Associated Protein-4 Regulate Its Nuclear Translocation and DNA Binding

Table 1

Mutant constructs used to study CKAP4 phosphorylation and palmitoylation. CKAP4 mutants that mimic constitutive depalmitoylation and various states of serine (S3, S17 and S19) phosphorylation were generated to determine their effect on the subcellular distribution of CKAP4 in response to APF. CKAP4SΔE translocated from the PM to the nucleus in response to APF; CKAP4SΔA localized to the PM but did not translocate to the nucleus in response to APF; none of the C100S mutants were expressed on the PM; CKAP4C100S/SΔE was expressed in the nucleus. The results indicate that CKAP4 must be palmitoylated for PM expression and depalmitoylated and phosphorylated for translocation to the nucleus. A summary of these results are provided in the table.

NameMutationsComments posttranslational modificationsResting distributionDistribution after APF

wild-type (WT) CKAP4noneexpressed or endogenousPM, ER> nucleus
CKAP4 C100SC100Sconstitutively depalmitoylatedER= ER
CKAP4 SΔAS3A, S17A, S19Aconstitutively dephosphorylatedPM, ER= PM, ER
CKAP4 C100S/SΔAC100S, S3A, S17A, S19Aconstitutively depalmitoylated, constitutively dephosphorylatedERER
CKAP4 SΔES3E, S17E, S19Emimics phosphorylationPM, ER> nucleus
CKAP4 C100S/SΔEC100S, S3E, S17E, S19Econstitutively depalmitoylated, mimics phosphorylationNucleus= nucleus

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