Poly(ADP-ribose) polymerase family member 16 (PARP16)

Poly(ADP-ribose) polymerase family member 16 (PARP16) is a tail-anchored, endoplasmic reticulum (ER)-associated enzyme that catalyzes the mono-ADP-ribosylation of target proteins, including critical ER stress sensors such as PERK and IRE1α, leading to their activation during the unfolded protein response (UPR)[1][2][4][5]. PARP16 also inhibits protein translation by ADP-ribosylating ribosomal subunits, and is implicated in regulating nucleocytoplasmic transport through modification of karyopherin-β1[1][2]. Additionally, PARP16 mono-ADP-ribosylates vascular endothelial growth factor (VEGF) in the ER, priming it for further modifications that modulate angiogenesis[1]. Recent evidence implicates PARP16 in maladaptive cardiac remodeling under conditions of pressure overload, suggesting relevance to cardiovascular disease[1]. PARP16 is classified as an enzyme within the ADP-ribosyltransferase and poly(ADP-ribose) polymerase family, with key roles in cellular stress responses, protein modification, translation regulation, and disease pathogenesis.

Other names

ARTD15pART15C15orf30PARP-16FLJ20509FLJ25281ADP-ribosyltransferase diphtheria toxin-like 15Protein mono-ADP-ribosyltransferase PARP16PART15PAR16_HUMAN

PARP16 inhibits protein translation by mono-ADP-ribosylating ribosomal proteins. It activates ER stress sensors like PERK and IRE1α through mono-ADP-ribosylation, thereby promoting the unfolded protein response. Additionally, it primes VEGF for further poly-ADP-ribosylation to modulate angiogenesis.