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- Table of Contents
Facts about Ras-related protein Rab-13.
That Rab is involved in endocytic recycling and modulates the transfer to the plasma membrane of transmembrane proteins such as the tight junction protein OCLN/occludin. Thereby, it modulates the assembly and the activity of tight junctions.
Human | |
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Gene Name: | RAB13 |
Uniprot: | P51153 |
Entrez: | 5872 |
Belongs to: |
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small GTPase superfamily |
Cell growth-inhibiting gene 4 protein; growth-inhibiting gene 4 protein; Rab13; RAB13, member RAS oncogene family; RAS-associated protein RAB13; ras-related protein Rab-13
Mass (kDA):
22.774 kDA
Human | |
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Location: | 1q21.3 |
Sequence: | 1; NC_000001.11 (153981605..153990644, complement) |
Detected in several types of epithelia, including intestine, kidney, liver and in endothelial cells.
Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell junction, tight junction. Golgi apparatus, trans-Golgi network membrane. Recycling endosome membrane. Cell projection, lamellipodium. Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions (PubMed:8294494). Relocalizes to the leading edge of lamellipodia in migrating endothelial cells (By similarity).
If you're interested in learning more about RAB13 and the clinical applications of this novel gene-marker, read the rest of this article. This article will cover Molecular Targets, Methods, and Clinical Applications. You'll also learn how to use this gene-marker combination to find new treatments for a range of diseases and conditions. It is an exciting time for research in the field of biomarkers.
The apical and basolateral membranes are specialized regions of the cell, and proteins containing these proteins are restricted to specific areas. In the case of RAB13, however, both apical and basolateral membranes are involved, and both proteins are present in the cytoplasm and on the lateral membrane. Therefore, the cellular distribution of RAB13 and the corresponding membrane proteins is altered by Rab13 mutants.
The polarisation of RAB13 mRNAs influences translation, local assembly of migratory machinery, and motile cell polarity. The mRNA localisation of RAB13 in EC protrusions was detected by using puromycinilation-proximity ligation assays. In addition, puromycinilation-PLA-based RNA-seq experiments showed that the nascent protein was a product of local translation. Puromycinilation-PLA detection of the nascent protein also excluded the presence of nascent proteins transported from the cell body to protrusions.
Molecular Targets of the RAB13 markers are largely conserved between cell types and may be an important mechanism for the coordinated regulation of complex morphogenetic events. Five-cluster k 5 mRNAs encode highly dynamic membrane trafficking and small GTPases that influence cell motility. Localised translation is also thought to be a crucial component of a coordinated effort to regulate actin dynamics and membrane protrusion at the leading edge.
Molecular Targets of the RAB13 markers are essential for the detection of disease-causing mRNAs. The three-letter UTR of the RAB13 mRNAs play a critical role in the polarisation of mRNAs in different cell types. Thus, Rab13 is a valuable tool for cancer researchers. Its polarised localisation in ECs is highly conserved across species and tissues.
The coding sequence of the human HBB gene was tagged with the RAB13 3'UTR and MS2 hairpin repeats. These hairpin repeats are usually confined to the nucleus. ECs expressed this reporter system in a manner similar to that of the mRNAs, thereby confirming the potency of the RAB13 3'UTR in localising mRNA.
Rab GTPases are important for the progression of cancer and are attractive therapeutic targets. Rab GTPases regulate vesicular transport along the cytoskeleton and function with tethering proteins within a membrane fused with the target compartment. Rab GTPases also regulate autophagy and metabolism. Drug resistance is a major concern in the face of tumor progression, and selective targeting of Rab GTPases might help in this regard.
The RAB13 gene has multiple functions in the cell. It controls the transport of EGFR to the cell membrane. It also controls the fusion and growth of lipid droplets. Rab8a is also involved in the development of the MDR in cancer cells. Rab5a and Rab21 are important in regulating EGFR expression in cancer cells. The ABCG2 gene is also involved in the development of MDR.
The RAB13 marker has recently been discovered in human cells. Its RNA content is abundant in peripheral tissues and contributes to various modes of cell migration. The RNA of the RAB13 gene is translated into protein by multiple pathways and is a critical factor in the phenotype of the encoded protein. Further, studies have shown that this protein is involved in the differentiation of various cancer cell types. In addition to its phenotypic characteristics, the RAB13 marker has important clinical applications.
Single cells were cultured on collagen matrices and were labeled with a Cherry-NLS fluorescent protein to mark nuclei. RAB13 RNA was then added to these cells and they were induced to migrate through the Matrigel plug. Serial imaging sections were obtained at various depths of the Matrigel plug to determine whether cells were reaching different areas. The RNA content of the RAB13 marker has been found to correlate with lung cancer status, smoking status, and gender.
The RAB13 gene is a member of the Rab family of small GTPases. It is involved in membrane trafficking and has an inverse correlation with survival in cancer. RAB13 is required for cell migration and invasion and its levels in plasma membranes inversely correlate with tumor prognosis. Multiple pathways are thought to function through RAB13, including activity-dependent recycling of integrins, modulation of actin-binding proteins at the leading edge, and cell migration.
The RAB13 gene product is a small, nonpolarised GTPase that is expressed in the cytoplasm and extracellular matrix of various types of cells. This gene may function as a receptor that delivers proteins to the surface. However, definitive functions of RAB13 remain elusive. In the present study, we used the RAB13 gene product as a marker to investigate the role of RAB13 in lung cancer.
The localisation of RAB13 mRNA to protrusions in vivo is conserved. Loss of this targeting induces mispatterning of migrating blood vessels in zebrafish. By using a mRNA probe, we were able to identify the mRNA responsible for localising RAB13 to a specific cell type. However, the results of this study are incomplete because the RAB13 protein is not present in the zebrafish telomere.
The RAB13 3'UTR consists of a minimum of 192 nt LE with four motif repeats. Deletion of individual motifs did not affect the localisation of RAB13. We suggest that different cluster k 5 mRNAs may require different minimal requirements for these motifs. These findings are consistent with previous research that shows that the RAB13 protein is required for accurate RNA sequencing.
In order to perform these studies, we used the RAB13 gene product to detect the mRNA of ECs. We found that ECs with RAB13 LE had highly polarised filopodia extensions in contrast to their counterparts. Furthermore, the RAB13 gene product showed a significant increase in overall frequency of filopodia in mutant ECs. Therefore, RAB13 gene expression in human cells is highly dependent on the tight control of RAB13 mRNA localisation.
Rab8 and Rab13 are largely conserved in tissues, and their expression has been linked to many diseases. Rab13 is required for the detection of many pathogens and is involved in the regulation of inflammatory response. Rab8 and Rab13 share similar roles in various diseases, and a decrease in either of these proteins will result in a reduction in the expression of both RAB13 and RAB8.
A single-cell culture of BHK cells was co-transfected with pCI-neo-Myc. This was followed by IP. This assay represents three independent experiments. The asterisks indicate non-specific bands. If the RAB13 gene is present in the cell population, then the cells are positive. Rab8A Q67L co-localized with RAB13.
In a study on E-cadherin and Rab13, the RAB8-JRAB/MICAL-L2 complex regulates the transport of occludin and E-cadherin. The RAB8-JRAB/MICAL-L2 complex also regulates the transport of claudin-1 and occludin. Rab13 depletion prevented E-cadherin from being transported to the PM.
PMID: 8294494 by Zahraoui A., et al. A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells.
PMID: 8375503 by Joberty G., et al. Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.