Identification of B56α, B56γ and BAP1 as PRR14L binding partners

Truncating mutations have been previously described in PRR14L associated with acquired isodisomy of chromosome 22 in myeloid neoplasms. Very little is known about the function of PRR14L, but previous work showed localization to the midbody and binding to KIF4A. Here we confirm binding of PRR14L to PP2A components B56α and B56γ. Similar to the related protein PRR14, PRR14L binds B56α via a conserved short linear motif within the C-terminal Tantalus domain. We also confirmed binding to BAP1, which forms the H2A deubiquinating complex PR-DUB with ASXL1, thereby linking PRR14L to a protein with established leukemogenic significance. AlphaFold data predicts PRR14L structure to be largely disordered, consistent with a possible role as a scaffold protein.