Ankrd13a, ankyrin repeat domain 13a, is involved in multiple biological processes. It plays a role in TNF signaling, acting as a component of complex-II to set a higher signal threshold for TNF-induced cytotoxicity, thereby controlling the early cell-death checkpoint [1]. It also has implications in processes like cell migration, as miR-204 targets Ankrd13A to regulate mesenchymal neural crest and lens cell migration by controlling focal cell adhesion formation and distribution [4].

In TNF signaling, Ankrd13a deficiency promotes the formation of death-inducing complex-II without affecting NF-κB activation, turning the response to TNF from survival to death. Ankrd13a binds to ubiquitinated-RIP1 via its UIM, limiting the association of FADD and caspase-8 with RIP1 [1]. In acute myeloid leukemia, lncRNA USP30-AS1 promotes cell survival by cis-regulating Ankrd13A, and Ankrd13A may contribute to immune escape by inducing HLA-I internalization [2]. In breast cancer, CYYR1 promotes the degradation of WWP1 and directs polyubiquitinated WWP1 toward lysosomal degradation through binding to Ankrd13A [3].

In summary, Ankrd13a is crucial in regulating cell-death checkpoints, cell migration, and has implications in cancer-related processes. Studies, such as those on its role in TNF-induced cell death, leukemia cell survival, and breast cancer-related protein degradation, have provided insights into its functions. These findings suggest that Ankrd13a could be a potential target for therapeutic intervention in diseases where its dysregulation occurs.