UBAP2L Antibodies

Ubiquitin-associated protein 2-like (UBAP2L)

Plays an essential role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs). .

Gene Information

Human
Gene Name:	UBAP2L
Uniprot:	Q14157
Entrez:	9898

Family

Belongs to:
No superfamily

Alternative Names

FLJ42300; KIAA0144NICE-4; NICE4; Protein NICE-4; ubiquitin associated protein 2-like; ubiquitin-associated protein 2-like

Molecular Weight

Mass (kDA):
114.535 kDA

Genomic Context

Human
Location:	1q21.3
Sequence:	1; NC_000001.11 (154220172..154271510)

Tissue Specificity

Ubiquitous.

Diseases

• Neuroblastoma
• Neurodegenerative Disorders
• Infertility

Pathways

• Fertilization

PTMs

• Acetylation

• Methylation

• Phosphoprotein

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/UBAP2L

Best Uses of the UBAP2L Marker

The UBAP2L molecule is one of a few novel BMI1-interacting protein and is required for stress granule assemblage. It is useful for identifying stress-related genes, including apoptotic proteins and cytokines. Below are some of the best uses for this marker, and how they can be used to aid scientists in their research. They are also useful in the development of new therapies and drugs.

UBAP2L a novel BMI1 interacting protein

The UBAP2L gene plays a significant role in regulating complex assembly during mitosis. It is implicated as a regulator of bipolar disorder, anorexia and other neurodegenerative conditions. The mechanism of UBAP2L action is still unknown. Further research is needed to determine the function of this gene.

UBAP2L regulates several key cell cycle regulators as well as tumor suppressors. This promotes cell growth and proliferation. It activates PI3K/Akt signaling pathway, and increases expression of P65 (SP1) and SP1. These effects are associated with epithelial-mesenchymal transition and cell proliferation. Overexpression of UBAP2L can also promote migration and invasion and maintain metastatic potential. UBAP2L may also bind the BMI1-dependent transcriptional repressor SNAIL1, which is strongly associated to cancer progression.

UBAP2L can be described as a gene encoded at the region of 1q21 by the KIAA0144 genetic code. Marenholz and co-workers discovered it in 2001. The gene encodes five types of UBAP2L. Despite its versatile roles, UBAP2L can be linked to a variety od cancer-related disease.

MiR-148b-3p is an inhibitor of UBAP2L that has anti-tumor actions in gastric carcinoma cells. MiR148b-3p represents a new target of UBAP2L. Moreover miR148b-3p expression in gastric cancer cells was found to be negatively correlated with UBAP2L. The findings indicate that UBAP2L plays an important role in gastric cancers.

The discovery of UBAP2L opened up new avenues for cancer research. Several studies have suggested that UBAP2L plays multiple roles in various signaling pathways. These functions require further research to determine the molecular mechanisms. This gene may be a promising target to develop future cancer therapies as it is expressed more in human tissues. Its multiple functions in normal, and pathological, conditions could make it a key for the development of new therapies.

Previously, it was reported that UBAP2L, a protein, functions in the Polycomb Complex, a family transcription factors. Although the exact mechanism of UBAP2L remains elusive, it is believed to be involved with the development of neuronal and nerve cells in the spinal column. This research is for anyone who has ever wondered how the brain grows.

To detect UBAP2L mRNA, and miR148b-3p expression, we used a real time PCR method. The UBAP2L ORF gene sequence was cloned in pcDNA3.1 vector by HindIII, XhoI restriction enzymes. Next, we used miR148b-3p mimics to decrease the activity for the luciferase reader. The levels of UBAP2L expression were lower in AGS cells than in normal gastric mucosa cells.

These results support our hypothesis that BMI1 induces extensive expansion of PMBCs in patients with SF. This study shows that this gene also plays a role in the differentiation of human erythroids from CD34+ HSPCs. UBAP2L, a novel BMI1-interacting proteins, may help us to understand this gene.

It is necessary for stress-granule assembly

Stress granules (SGs) are discrete assemblies of stalled mRNPs. These complexes can be formed by RNA binding proteins, which recruit mRNPs into forming SGs. This marker, UBAP2L, is required for stress granule assembly and disassembly. It also controls recruitment of mRNPs into SGs.

Previous research has implicated UBAP2L for the formation of stress granules, and the development neurodegenerative diseases. Knocking out UBAP2L failed to induce nuclear translocation. Deletion of the FG–LA domain did not prevent nuclear translocation. However, UBAP2L was unable to maintain its nuclear localization signal if the DUF domain was deleted. The protein can also interact with docking protein and regulate transcription.

Various cancers have been linked to the expression of UBAP2L. Previously, this marker was initially identified in human sperm, but it has been linked to various types of cancer. In the study reported here, it was discovered that UBAP2L is required for mitosis and accurate chromosome distribution. These findings are consistent from previous studies. However, it is unclear what role UBAP2L played in stress granule formation.

UBAP2L was significantly reduced in the formation of SGs upon H2O2 treatment, but not increased sorbitol-induced SG production. Moreover, UBAP2L inhibition delayed SG disassembly in the absence of H2O2. After H2O2 withdrawal, cells that were knocked down by UBAP2L showed greater effectiveness. It also delayed the disassembly SGs after recovery.

The RGG motif in UBAP2L interacts with other SG proteins. This protein recruits many other SG -nucleating proteins such as G3BP1/2. These proteins are crucial for SG assembly. A loss of a single RGG mole in UBAP2L will decrease SG formation.

UBAP2L methylation decreases during stress and increases after stress recovery. PRMT1 is a molecular device that controls this process. It monitors the methylation UBAP2L arginine. These findings suggest that UBAP2L arginine methylation is critical for stress granule assembly. It is not clear which proteins regulate PRMT1.

It is a novel marker to stress granule assembly

Inflammatory cell contain dynamic membrane-less condensates (called stress granules, or SGs), which transiently assemble. The SGs are biphasic in architecture, with a conserved core containing translational-related proteins and RNA-binding domains, and a shell that contains a variety of different components. These components differ in species and developmental stages, but they are consistent with a role in cellular response to various stresses.

The process of stress-granule assembly involves the creation of stable core structures, and the subsequent assembly larger stress granules. These granules can contain more than one core, and their size distribution is similar from 15 to 120 min of stress. This suggests that core development does not occur at an early stage, as previously thought. Instead, IDRs with high local concentrations create a stress-granule shell.

Recent research found that 1,6Hexanediol produced a yeast-like granule assembly. The granules also reassembled in a matter of minutes, which was sensitive for cycloheximide (a drug known to inhibit stress granule formation). The induced granules also showed stable interactions with a number of proteins, including G3BP1 or PABP1. These results highlight the importance and potential value of UBAP2L in stress granule assembly.

G3BP has also been proven to stop HIV replication and sequester viral DNA. G3BP in cancer is associated to poor prognosis because it is overexpressed within bone sarcoma cell and lung tissues. G3BP can be downregulated to reduce stress granule formation, tumor invasion and metastasis. It has been linked to Ras-GAPSH3 and its role in stress granule creation in cancer.

UBAP2L is a novel protein that is found in the stress granule core. In a laboratory setting, the liquid-liquid phase separation occurs between the mRNPs in stress granules. Although this separation can lead to a stable core, the mechanism behind it is not known. In vivo, stress granules undergo a similar process.

Stepwise, stress granules are disassembled. After core clearance and shell destruction, the granules are subject to a stepwise disassembly. These small assemblies become microscopic undetectable in the same time span. It is therefore important to distinguish UBAP2L with other markers in order monitor stress granules assembly in the laboratory.

UCAP2L may be a novel marker to regulate stress granule aggregation, but it has already been identified as a potential biomarker for ER Stress. It can also be used as a candidate for a stress-granule nucleus that is controlled by specific signaling clues. Its role is being expanded in stress response and will likely become a key component for future studies.

The UBAP2L is an innovative candidate for stress granule assemblage that could be useful in the identification of a new gene associated this process. In addition to its role in stress granule assembly, UBAP2L also regulates the production of phosphoRin, which is a major component of the stress response. The Sec16/phosphoRin complex recruits Rin and allows it to bind to another partner. This may make Sec16 a stress-granule marker that's specific for amino acid starvation.