Chromodomain Y-like protein 2 (CDYL2)

Chromodomain Y-like protein 2 (CDYL2) is a member of the chromodomain Y protein family, distinguished by having both a chromodomain (CD) at its N-terminus and an enoyl-CoA hydratase-like domain at its C-terminus[1]. The chromodomain binds methylated histone tails, particularly H3K9me3—a marker of repressed chromatin—while the ECH domain is associated with fatty acid metabolism and may contribute to gene silencing and cancer progression[1]. CDYL2 exists as multiple isoforms through alternative splicing; key isoforms localize to distinct nuclear compartments and exert contrasting effects in breast cancer: one promotes proliferation, while another represses metastasis-related genes[1]. Functionally, CDYL2 is an adaptor that connects centromeric chromatin marks (H3K9me3) to key mitotic regulators (CHAMP1, POGZ), ensuring proper chromosome segregation and genome stability during cell division[2]. Knockdown of CDYL2 in cancer cells impairs cell growth, induces apoptosis, and produces nuclear and mitotic defects, highlighting its essential role in cell cycle regulation[2]. Differential CDYL2 expression is noted in several tissues, including testis, prostate, spleen, and leukocytes, with involvement in both normal development (e.g., spermatogenesis) and disease contexts (e.g., cancer and neurodevelopmental disorders)[1][2].

Other names

Chromodomain Y-like 2CDY-like 2PCCP1FLJ38866Prostate cancer candidate protein 1

No approved drugs directly target CDYL2; known mechanisms involve indirect regulation by drugs that modulate its expression (e.g., mood stabilizers affecting transcript levels)[1].