Overview:

PSMD14 is a deubiquitinating enzyme within the 19S proteasomal subunit. It is specific for K63-Ub chains releasing polyubiquitin chains from the polyubiquitinated protein substrates of the proteasome. PSMD14 regulates macroautophagy by controlling Golgi-to-ER retrograde transport (1). It also plays a critical role in physiological and pathological processes such as DNA damage repair, tumor formation and inflammation (2). PSMD14 is significantly upregulated in HCC and lung cancer, and indicates poor prognosis (2, 3). Downregulation of PSMD14 causes cell cycle arrest leading to senescence and apoptosis, therefore it is a potential target for small molecule inhibitors in cancer therapeutics (2).

Gene Aliases:

Proteasome 26S Subunit, Non-ATPase, POH1, 26S Proteasome Non-ATPase Regulatory Subunit

Genbank Number:

NM_005805

References:

1. Bustamante, H.A. et al: The proteasomal deubiquitinating enzyme PSMD14 regulates macroautophagy by controlling Golgi-to-ER retrograde transport. Cells 2020; 9(3), 777.

2. Zhang, L. et al: Upregulation of deubiquitinase PSMD14 in lung adenocarcinoma (LUAD) and its prognostic significance. Journal of Cancer. 2020; 11(10):2962-2971.

3. Jie, L. et al: Deubiquitinase PSMD14 enhances hepatocellular carcinoma growth and metastasis by stabilizing GRB2. Cancer Letters. 2020; 469:22-34.