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- Table of Contents
Facts about Lethal(2) giant larvae protein homolog 1.
Involved in axonogenesis via RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane. .
Human | |
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Gene Name: | LLGL1 |
Uniprot: | Q15334 |
Entrez: | 3996 |
Belongs to: |
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WD repeat L(2)GL family |
DLG4lethal giant larvae (Drosophila) homolog 1; HUGL; HUGL1; HUGL-1; Human homolog to the D-lgl gene protein; lethal giant larvae homolog 1 (Drosophila); lethal(2) giant larvae protein homolog 1; LLGL
Mass (kDA):
115.418 kDA
Human | |
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Location: | 17p11.2 |
Sequence: | 17; NC_000017.11 (18225593..18244875) |
Expressed in brain, kidney, and muscle but is barely seen in heart and placenta. Down-regulated or lost in all cell lines and in most of the tumor samples analyzed. Loss was associated with advanced stage of the disease.
Early endosome membrane. Golgi apparatus, trans-Golgi network membrane. Golgi apparatus membrane. Cell projection, axon. Cytoplasm, cytoskeleton. Localized to the lateral membrane during the polarization and formation cell-cell contacts. Enriched in developping axons (By similarity).
The LLGL1 gene marker is a versatile genetic tool that can be used for the detection of LLGL1 low-density lipoprotein ligand like protein. The LLGL1 genetic code encodes for a particular protein. Several people are genetically predisposed to LLGL1 protein ligands. Boster antibodies are highly precise and have been widely cited in the last 25 years. They have been validated on immunohistochemistry, ELISA, and Western Blotting.
The histology for mice deficient in cell polarity protein LLGL1 looks similar to human Periventricular Heterotopia. This disease is marked by an abnormally deposited layer of gray matter. Mice lacking the Llgl1 genes lack a cell-cell adhesion structure molecule, which regulates the localization and positioning of neural stem cells.
Although Llgl1's role in cardiac development is still unclear, research has focused on its role in regulation Hippo-Yap signaling by cardiomyocytes. In addition, recent findings have indicated that Llgl1 may be a potential modulator of Hippo-Yap signaling, an area of increasing interest in cardiac regeneration.
In addition to being a receptor for gemcitabine, LLGL1 is also implicated in the regulation of Yap protein levels and the transcriptional activity of zebrafish cardiomyocytes. This research shows Llgl1 regulates Yap protein and YAP -TEAD expression. Although the exact mechanism of LLGL1 remains ambiguous, the function and importance of the LLGL1 indicator is critical for maintaining gemcitabine tolerance.
Interestingly, LLGL1 inhibits the degradation of the proto-oncogene YAP. It is essential for maintaining cell junctions with the right protein composition. This protein is crucial for intercalated discs of cardiomyocytes and adherent junctions in epithelia. Yap phosphorylates ERK2 if Llgl1 gets deleted.
Drosophila's LLGL1 marker plays a role in tumor suppression. It also improves response to gemcitabine in PDAC-patients. In addition, it is implicated in apoptosis. It has been found in Drosophila and warts have been detected. It is important to understand the role of the LLGL1 gene in regulating the expression of hENT1 & hENT2 genes in humans.
Recent research has shown that Yap activity is modulated by the LLGL1 gene. This protein is essential for maintaining cell junctions. The loss of Llgl1 causes Yap to be delocalized, phosphorylated and eventually degraded by ubiquitin ligation.
Recent studies show that LLGL1 promotes composition of cell-junction complexes and protects heart muscle cells from phosphomediated proteasome targeted. Recent findings suggest that LLGL1 has a role in cancer metastasis-free survival. This process is regulated by LLGL1 and no other gene.
Researchers have previously shown that LLGL1 regulates Hippo-Yap activity in cardiac cells. Consequently, it represents a potential mechanism for modulating Hippo-Yap signaling, an area of growing interest in cardiac regeneration. A new LLGL1 mRNA might help improve cardiac rehabilitation. These studies are just the beginning. However, the future of cardiovascular research relies on the results of ongoing studies.
YAP ChIP–Seq and RNA–seq studies have demonstrated that the Llgl1 gene regulates Yap protein expression. These studies reveal that LLGL1 regulates Yap TEAD transcriptional activity. These findings suggest that the LLGL1 gene could also regulate Yap protein levels. Nevertheless, it remains unclear exactly how Llgl1 regulates the activity of Yap.
PMID: 7542763 by Strand D.J., et al. A human homologue of the Drosophila tumour suppressor gene l(2)gl maps to 17p11.2-12 and codes for a cytoskeletal protein that associates with nonmuscle myosin II heavy chain.
PMID: 8565641 by Koyama K., et al. The human homologue of the murine Llglh gene (LLGL) maps within the Smith-Magenis syndrome region in 17p11.2.