TRIM28 Antibodies

Transcription intermediary factor 1-beta (TRIM28)

Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the rise in H3K9me, the reduction in histone H3'Lys-9 and'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression.

Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation.

Gene Information

Human
Gene Name:	TRIM28
Uniprot:	Q13263
Entrez:	10155

Family

Belongs to:
TRIM/RBCC family

Alternative Names

E3 SUMO-protein ligase TRIM28; EC 6.3.2.-; FLJ29029; KAP1; KAP-1; KAP1KRAB-associated protein 1; KRIP-1; Nuclear corepressor KAP-1; RNF96; RNF96KRAB-interacting protein 1; TF1B; TIF1B; TIF1-beta; TIF1BRING finger protein 96; transcription intermediary factor 1-beta; transcriptional intermediary factor 1-beta; TRIM28; tripartite motif containing 28; tripartite motif-containing 28; Tripartite motif-containing protein 28

Molecular Weight

Mass (kDA):
88.55 kDA

Genomic Context

Human
Location:	19q13.43
Sequence:	19; NC_000019.10 (58544064..58550722)

Tissue Specificity

Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.

Subcellular Localizations

Nucleus. Associated with centromeric heterochromatin during cell differentiation through CBX1.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Cell Transformation, Neoplastic
• Ataxia
• Ataxia Telangiectasia
• Leukemia
• Telangiectasis
• Immunologic Deficiency Syndromes
• Malignant Neoplasm Of Breast
• Embryonal Carcinoma
• Leukoencephalopathy, Progressive Multifocal
• Mammary Neoplasms

• Melanoma
• Neoplasm Metastasis
• Autoimmune Reaction
• Hiv Infections
• Hypoxia
• Acute Promyelocytic Leukemia
• Stress, Psychological

Interacting Proteins

• Cbx1
• CBX3
• Cbx3
• CBX5
• CHD3

• MAGEA2
• MAGEA3
• MAGEA6
• MAGEC2
• MAGEE1

• NCOR1
• SENP7

Pathways

• Gene Silencing
• Methylation
• Cell Cycle
• Chromatin Remodeling
• Dna Repair
• Dna Methylation
• Cell Differentiation
• Cell Proliferation
• Cell Growth
• Interphase
• Histone Deacetylation
• Dna Replication
• Cell Cycle Checkpoint

• Double-strand Break Repair
• Mitosis
• Localization
• Demethylation
• Cell Death
• Dna Demethylation
• Spermatogenesis

PTMs

• Phosphorylation
• Methylation
• Acetylation
• Sumoylation

• Deacetylation
• Dephosphorylation
• Demethylation
• Cleavage

• Ubiquitination

Research Areas

• Phospho-Specific

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TRIM28

Boster Bio - Best Uses Of The TRIM28 Marker

The TRIM28 marker is an MDM2-binding protein that is important for cell homeostasis and is known to be a transcriptional repressor. It is also an inhibitor of mitophagy-associated microRNAs. Here are the best uses for TRIM28. The Boster Bio guide will help you determine which conditions to use to achieve your desired results.

TRIM28 is a novel MDM2-binding protein

In this study, researchers have shown that the MDM2-binding protein TRIM28 regulates tumor growth in mice. They injected either TRIM28WT or TRIM28KD cells into athymic nude mice or the MCF-7 cell line, and measured tumor growth weekly for a period of 7-8 weeks. In the TRIM28KD (sh#1) mice, TRIM28 expression was decreased, and they confirmed this by RT-qPCR.

In addition, knockdown of TRIM28 inhibits cadherin-dependent migration. Moreover, it is required for downregulation of selected mesenchymal markers. TRIM28 is required for the inhibition of the cadherin switch, as shown by RPPA analysis. The TRIM28 coiled-coil domain is required for this function.

TRIM28 is critical for maintaining the stem cell phenotype of embryonic stem cells (ESCs) and induced pluripotent stem cells (iPSCs). In addition, mice lacking Trim28 die shortly before gastrulation. Recent studies have shown that this protein plays a role in autophagy, a process that maintains the stem-like phenotype of breast cancer cells.

Inhibition of cellular growth by TRIM28 is mediated by a cancer-specific ubiquitin ligase. This protein targets AMPK, the master regulator of metabolic/energy homeostasis, and regulates the growth of cancer cells by regulating the mitochondrial biogenesis. Knockdown of TRIM28 resulted in increased levels of AMPK protein and decreased stability of AMPK.

The gene is expressed in the tumor tissues of patients with BRCA mutations. TRIM28 expression is distinct between BRCA intrinsic and luminal subtypes, with TRIM28 overexpression associated with triple-negative tumors. In the TCGA BRCA, patients with TRIM28 high expression are more likely to have triple-negative tumors. The TRIM28 gene expression level was 4.2E06 in the dataset from Stickeler et al.

It is a transcriptional repressor

The TRIM28 gene is a member of the Kruppel transcription factor family. Initially identified as a polypeptide, TRIM28 is a multidomain transcriptional repressor that interacts with the Kruppel transcription factor family. It is now recognized as a versatile transcription factor associated with genes scattered throughout the genome. This article will discuss some of the most notable functions of TRIM28.

A methylation-sensitive interaction screen reveals that TRIM28 recruits to the methylated allele of imprinting control regions, which contain a series of genes that act together to regulate the final expression of imprinted genes. These genes depend on the KRAB domain zinc finger protein ZFP57, which generates an epigenetic remodeler complex that interacts with histone deacetylases and methyltransferases.

The TRIM28 mechanism is compatible with established pathways for Pol II pausing, including recruitment of P-TEFb to the activated gene and phosphorylation of NELF. Phosphorylation of TRIM28 has been observed in DNA repair studies, and this modification has a significant impact on the structure of nucleosomes. However, it remains unclear whether or not TRIM28 is directly involved in pausing transcription.

TRIM28 is a multidomain protein with numerous roles in transcription and DNA repair. It plays novel roles in regulating transcriptional control, DNA repair, and Pol II elongation. It stabilizes the pausing of RNA polymerase II (Pol II) near the transcriptional start site. It also responds rapidly to the signals that accompany transcriptional activation. Therefore, the reduction in TRIM28 levels could lead to increased basal elongation and gene expression.

TRIM28 is critical for HIF-1-mediated transcription in hypoxic human breast cancer cells. HIF-1 recruits TRIM28 to HREs where it phosphorylates DNA-PKcs, which are two proteins whose function is to recruit DNA-PK to the HRE. TRIM28 and DNA-PK interact with HIF-1 and inhibit transcriptional elongation.

It promotes cell homeostasis

The TRIM28 marker has been implicated in the regulation of stem cell functions, and its role in cancer development and progression is well-understood. It acts as a tumor suppressor, and inhibits the expression of several genes. The TRIM28 marker is also involved in regulating cell homeostasis, thereby promoting apoptosis and cell division.

In addition to regulating cell homeostasis, Trim28 is a transcriptional corepressor. It belongs to a family of genes that interact with KRAB-containing zinc finger transcription factors and harbors SUMO E3 ligase activity. It plays a key role in several aspects of mammalian physiology, and has recently been associated with autophagy. Trim28 is involved in the regulation of the production of microRNAs that regulate autophagy-related genes.

The TRIM family of proteins has been shown to play multiple roles in biology and cellular function. They regulate cell proliferation, cell division, autophagocytosis, and metabolism. Several TRIM members are implicated in the promotion of cell homeostasis and stem cell phenotype, and a growing body of evidence suggests that they are essential for cancer stem cell self-renewal.

Previous studies have shown that the TRIM28 marker regulates genes that control lipid abundance and adipocyte function. This study found that trim28 gene expression was reduced in white and brown adipose tissue, but not in other tissues such as skeletal muscle or liver. These data suggest that Trim28 is an important regulator of cell homeostasis and is involved in the regulation of lipid metabolism.

Moreover, the TRIM28 adi-KO mice were found to have decreased levels of longer chain FA species and TG(48:x-54:x). These changes may be important for metabolic health. Furthermore, mice containing Trim28 adi-KO were found to have lower fasting blood glucose levels, consistent with increased insulin signaling. These changes are consistent with increased insulin signaling in the liver.

It inhibits mitophagy-associated microRNAs

The target of this study was the microRNA miR-137, which was found to be downregulated in blood serum of Alzheimer disease patients. This study also demonstrated that miR-137 inhibits the function of mitophagy receptors bound to the LC3 membrane. These findings provide important insights into the role of mitophagy in aging and human disease.

In tumor cells, the TRIM28 protein inhibits the production of microRNAs that target genes involved in mitophagy. By inhibiting the expression of these microRNAs, TRIM28 is able to support the proper mitophagy mechanism in erythropoiesis. It is unclear whether cancer cells also utilize the mitophagy mechanism.

TRIM28 is a novel MDM2-binding protein that contributes to the functional regulation of p53. It inhibits p53 acetylation, which leads to p53 degradation. The study also reveals that TRIM28 is an important target in cancer therapy. It is important to note that tumor cells that express TRIM28 are more likely to be cancer-susceptible.

TRIM28 also affects the transcriptional elongation of RNA. It stabilizes Pol II pausing close to the transcriptional start site. This enables Pol II to accumulate and prepare genes for induction. It also influences Pol II phosphorylation status, enabling rapid transcription of target genes. TRIM28 phosphorylation is required for Pol II release.

MiR-137 inhibits the autophagic degradation of mitochondrial proteins. This resulted in accelerated autophagic responses in hypoxia. However, the mechanism by which this microRNA is regulated remains unclear. It appears to function by inhibiting the autophagic response induced by fundc1 (CDS+3'UTR).

It regulates p53 function

TRIM28, a novel MDM2 binding protein, contributes to p53 function by inhibiting p53 acetylation. This inhibited acetylation eventually leads to the proteasomal degradation of p53. This inhibited p53 activity may also contribute to p53 function by regulating the epithelial to mesenchymal transition. TRIM28 is a multifunctional protein that regulates gene expression, autophagy, and p53 function.

Recent studies have demonstrated that the multi-domain TRIM28 protein is involved in cancer progression and stem cell maintenance. TRIM28 has also been implicated in the regulation of cancer stem cells and EMT. It may have anti-tumorigenic implications. Future studies should clarify the role of TRIM28 in tumorigenesis. Further analysis will help us understand whether TRIM28 is an anti-cancer target.

TRIM28 functions as a scaffold for heterochromatin-inducing factors. This scaffolding activity of TRIM28 is dependent on its interaction with the repression domain of KRAB. Additionally, the TRIM28 protein is recruited by other proteins including the SETDB1 and NuRD complex proteins. These two proteins act to create a H3K9me3 mark on nucleosomes and deacetylate histone proteins. TRIM28 is also recruited by HP1 protein, which binds to its PxVxL motif.

In a recent study, scientists discovered that TRIM28 inhibits the activity of the mitophagy-associated gene FBP1. This target protein is involved in gluconeogenesis, and high expression of TRIM28 increased glucose consumption and lactate production. The findings suggest that TRIM28 regulates p53 function by modulating the metabolic state of cancer cells. Further research is needed to determine whether TRIM28 has a role in tumor development and metastasis.