Browse our Tripartite Motif Containing 28 Proteins (TRIM28)

Human Tripartite Motif Containing 28 (TRIM28) interaction partners

1. Genes co-repressed by TRIM28 and FAM208A are evolutionarily young, or exhibit tissue-specific expression, are enriched in young L1s, and display evidence for regulation through LTR promoters. Finally, we demonstrate that the HUSH complex is also required to repress L1 elements in human cells.

2. Authors identify a viral mechanism for the counteraction of KAP1 (show CDKN3 Proteins) in which interference with the KAP1 (show CDKN3 Proteins) phosphatase protein phosphatase 1 (show PPP1CB Proteins) (PP1 (show PPA1 Proteins)) by the AAV2 Rep proteins mediates enhanced phosphorylation of KAP1 (show CDKN3 Proteins)-S824 and thus relief from KAP1 (show CDKN3 Proteins) repression.

3. Evaluation of the potential mechanism demonstrated that TRIM28 promoted cervical cancer cell growth by activating the mammalian target of rapamycin (mTOR (show FRAP1 Proteins)) signaling pathway. In support of this finding, TRIM28-induced cell proliferation was abolished by treatment with everolimus, a specific mTOR (show FRAP1 Proteins) inhibitor

4. TRIM28 employs KRAB-ZNFs to evoke epigenetic silencing of its target differentiation genes via H3K9me3 and DNA methylation (show HELLS Proteins).

5. Study describes germline mutations and loss of function of TRIM28 in familial Wilms tumours, along with somatic loss of function in a non-familial Wilms tumour. Inactivation of TRIM28 provides the molecular basis for defining a previously described subtype of Wilms tumour, that has early age of onset and excellent prognosis.

6. Study identified TRIM28 among REST-interacting proteins, and suggested functional links between REST and TRIM28 during neuronal development and differentiation via induction of CTNND2 (show CTNND2 Proteins) expression.

7. Data indicate a mechanism in breast cancer cells that tripartite motif-containing 28 protein (TRIM28) enhances metastasis by stabilizing TWIST1 (show TWIST1 Proteins), suggesting that targeting TRIM28 could be an efficacious strategy in breast cancer treatment.

8. Gamma-H2AX (show H2AFX Proteins), phosphorylated KAP-1 (show CDKN3 Proteins) and 53BP1 (show TP53BP1 Proteins) play an important role in the repair of heterochromatic radon-induced DNA double-strand breaks.

9. Our data demonstrate that the downregulation of TRIM28 gene expression reduced the ability of CSCs to self-renew that resulted in significant reduction of tumor growth. Loss of function of TRIM28 leads to dysregulation of cell cycle, cellular response to stress, cancer cell metabolism, and inhibition of oxidative phosphorylation.

10. Cell proliferation and apoptosis were almost completely abolished in the PAa cells cotreated with TRIM28 siRNA and etoposide following knockdown of E2F1 (show E2F1 Proteins). The results of our study demonstrated that the combination of TRIM28 siRNA and etoposide may be effective against nonsmall cell lung cancer (NSCLC)and has the potential of being a new therapeutic tool for future treatment.

Mouse (Murine) Tripartite Motif Containing 28 (TRIM28) interaction partners

1. Results show that KAP1 maintains H3K9me3 at imprinting control regions and transposable elements and protects them from TETdependent hydroxymethylation.

2. regulation of epigenetic modifications coordinated by TRIM28 plays a crucial role in reprogramming process.

3. The interaction of repressor proteins Trim28 and YY1 (show YY1 Proteins) are involved in the silencing of Moloney murine leukemia virus.

4. an important role for TRIM28 in cells resisting transition between somatic and pluripotent states, is reported.

5. Nuclear factors that bind to genomic regions with "Sertoli Cell Signature" could functionally interact with SOX9 (show SOX9 Proteins); TRIM28 is a new SOX9 (show SOX9 Proteins) partner in fetal testes.

6. TRIM28 safeguards germline-to-soma inheritance of epigenetic features at other genomic regions in an exquisitely stage-dependent manner.

7. Data suggest that TRIM28 regulates the expression of a subset of lncRNAs.

8. Zygotic TRIM28 is essential for genomic imprinting. Secondary imprints were hypomethylated in TRIM28 mutants.

9. Trim28(+/D9) mutant mice exhibit a bi-modal body-weight distribution, with isogenic animals randomly emerging as either normal or obese and few intermediates.

10. Data suggest that interaction between KAP1 and the KRAB A (show ZNF223 Proteins) box of zinc finger protein 809 (ZFP809) is critical in KAP1-dependent control of gene silencing for ZFP809 targets.

Cow (Bovine) Tripartite Motif Containing 28 (TRIM28) interaction partners

1. Nuclear factors that bind to genomic regions with "Sertoli Cell Signature" could functionally interact with SOX9 (show SOX9 Proteins); TRIM28 is a new SOX9 (show SOX9 Proteins) partner in fetal testes.