Disease relevance of PUM2

• Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins [1].

High impact information on PUM2

• Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation [2].
• The repression is mediated by 3'UTR Pumilio-Binding Elements (PBEs), and by its binding protein Pumilio 2 (Pum2) [2].
• These results demonstrate that a reversible Pum2 interaction controls RINGO/Spy mRNA translation and, as a result, CPEB-mediated cytoplasmic polyadenylation [2].
• These data implicate PUM2 as a component of conserved cellular machinery that may be required for germ cell development [1].
• PUM2 pull-down methods combined with reverse transcription and RT-PCR confirmed that PUM2 does indeed bind P2P-R mRNA [3].

Biological context of PUM2

• Here, we report identification and characterization of RNA sequences to which PUM2 and DAZL bind [4].
• We mapped the domain of BOL that is required for dimerization and for interaction with PUM2 [5].
• These results suggest that P2P-R expression may be translationally regulated by PUM2 and that P2P-R may modulate translation by influencing ribosomal protein gene expression [3].
• PUM1 consists of 22 exons, spanning about 150 kb on chromosome 1p35.2, whereas PUM2 consists of 20 exons and spans at least 80 kb on chromosome 2p23-24 [6].
• Pum2 downregulation in neurons via RNA interference (RNAi) interferes with the formation of SGs during metabolic stress [7].

Anatomical context of PUM2

• We also show that in men, the NOS1 and PUM2 proteins are particularly abundant in germline stem cells [8].

Associations of PUM2 with chemical compounds

• This induction of SGs is dependent on the RNA-binding domain and a glutamine-rich region in the N terminus of Pum2 [7].

Enzymatic interactions of PUM2

• Identification and characterization of RNA sequences to which human PUMILIO-2 (PUM2) and deleted in Azoospermia-like (DAZL) bind [4].

Other interactions of PUM2

• Then, we used coimmunoprecipitation to isolate human transcripts specifically bound by PUM2 and DAZL and subsequently identified those that contain NRE-like sequence elements [4].
• Here, we demonstrate that human BOL forms homodimers and is able to interact with a PUMILIO homolog, PUM2 [5].
• Interaction of the conserved meiotic regulators, BOULE (BOL) and PUMILIO-2 (PUM2) [5].

Analytical, diagnostic and therapeutic context of PUM2

• Cloning and comparative sequence analysis of PUM1 and PUM2 genes, human members of the Pumilio family of RNA-binding proteins [6].

References