High impact information on TRIM69

• These results suggest that RNF36 may interact with PML and induce cell apoptosis [1].
• Treatment with the p38 inhibitor SB203580 resulted in the cytoplasmic translocation of RNF36 [1].
• Forced expression of RNF36 induces cell apoptosis [1].
• We suspect that RNF36 may play a role in germ cell homeostasis during spermatogenesis [1].
• The full-length RNF36 protein in both cell lines showed a speckled pattern in the nucleus [1].

Biological context of TRIM69

• Overexpression of full-length RNF36 in cells induced about half of the transfected cells to undergo cell death [1].
• In vitro phosphorylation analysis further suggested that RNF36 nuclear localization is under the control of phosphorylation, which might be mediated by p38 [1].
• RNF36 (ring finger protein 36; alias Trif), a member of the RING zinc finger protein family, is expressed in germ cells at round spermatid stages during spermatogenesis [1].
• Using degenerate oligonucleotide primers corresponding to the RING domain, we isolated a novel RING finger gene from the mouse testis cDNA library, which was about 1.8 kb and was termed Trif (testis-specific ring finger) [2].

Anatomical context of TRIM69

• Further analysis detected Trif transcripts in the testis from day 20 of the postnatal stage [2].

Associations of TRIM69 with chemical compounds

• To the Editor: role of MyD88 and Trif in acute allograft rejection: Glass half full or empty [3]?

Co-localisations of TRIM69

• Double-staining and coimmunoprecipitation analyses suggested that RNF36 colocalizes and interacts with PML [1].

Analytical, diagnostic and therapeutic context of TRIM69

• Northern blot analysis of adult multiple tissues indicated that Trif is expressed predominantly in the testis [2].
• In situ hybridization indicated that Trif is expressed in the round spermatids of the seminiferous tubules [2].

References