T101 DDH (Dihydrodiol Dehydrogenase)

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571.38 €

Known as:: T101 DDH (Dihydrodiol Dehydrogenase)
Catalog number:: mc-983
Product Quantity:: USD
Category:: -
Supplier:: Kamiya biomedical company
Gene target:: T101 DDH (Dihydrodiol Dehydrogenase)

Related genes to: T101 DDH (Dihydrodiol Dehydrogenase)

Gene:: KIAA0100 ^{NIH gene}
Name:: KIAA0100
Previous symbol:: -
Synonyms:: DKFZp686M0843, MGC111488, BCOX1, CT101, BCOX, FMP27
Chromosome:: 17q11.2
Locus Type:: gene with protein product
Date approved:: 2005-11-22
Date modifiied:: 2019-04-12

Related products to: T101 DDH (Dihydrodiol Dehydrogenase)

Related articles to: T101 DDH (Dihydrodiol Dehydrogenase)

BLTP2 bridges the ER and MVB for exosome biogenesis at SCAMP3-dependent ER contacts.
Multivesicular bodies (MVBs) contain intraluminal vesicles (ILVs) designated for degradation in lysosomes or release as exosomes for cell-to-cell communication. The mechanisms governing ILV/exosome formation are not fully understood. Here, we show that the integral endoplasmic reticulum (ER) membrane protein bridge-like lipid transfer protein 2 (BLTP2; KIAA0100) is indispensable for ILV/exosome formation and that secretory carrier membrane protein 3 (SCAMP3) recruits BLTP2 to ER-MVB membrane contact sites (MCSs) in a Rab5-dependent manner. Our results indicate that this recruitment is hindered by NEDD4-mediated ubiquitination of SCAMP3. Depletion of BLTP2 was found to impede ILV/exosome formation and selectively reduce the levels of cone-shaped phospholipids, including bis(monoacylglycero)phosphate (BMP), and of the BMP precursor phosphatidylglycerol (PG) within endosomes. BLTP2 knockout also hampered cell proliferation and tumorigenicity, which could be restored by supplementation with exosomes from wild-type cells. Our findings suggest that BLTP2 transfers the BMP/lysobisphosphatidic acid (LBPA) precursor PG to MVBs for BMP/LBPA synthesis and promotes ILV/exosome formation at SCAMP3-dependent ER-MVB MCSs. - Source: PubMed
Publication date: 2026/08/24
Wang JingruLi DongchenLiu YazhouZhou TiantianDeng LinJi Wei-Ke
Multiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics.
BLTP2/KIAA0100, a bridge-like lipid transfer protein, was reported to localize at contacts of the ER with either the plasma membrane (PM) or recycling tubular endosomes depending on the cell type. Our findings suggest that mediating bulk lipid transport between the ER and the PM is a key function of this protein, as BLTP2 tethers the ER to tubular endosomes only after they become continuous with the PM and that it also tethers the ER to macropinosomes in the process of fusing with the PM. We further identify interactions underlying binding of BLTP2 to the PM, including phosphoinositides, the adaptor proteins FAM102A/FAM102B, and N-BAR domain proteins at membrane-connected tubules. The absence of BLTP2 results in the accumulation of intracellular vacuoles, many of which are connected to the PM, pointing to a role of the lipid transport function of BLTP2 in the control of PM dynamics. - Source: PubMed
Publication date: 2025/09/03
Dai AnbangXu PengAmos ChaseFujise KenshiroWu YumeiYang HanEisen Julia NGuillén-Samander AndrésDe Camilli Pietro
Multiple interactions mediate the localization of BLTP2 at ER-PM contacts to control plasma membrane dynamics.
BLTP2/KIAA0100, a bridge-like lipid transfer protein, was reported to localize at contacts of the endoplasmic reticulum (ER) with either the plasma membrane (PM) or recycling tubular endosomes depending on the cell type. Our findings suggest that mediating bulk lipid transport between the ER and the PM is a key function of this protein as BLTP2 tethers the ER to tubular endosomes only after they become continuous with the PM and that it also tethers the ER to macropinosomes in the process of fusing with the PM. We further identify interactions underlying binding of BLTP2 to the PM, including phosphoinositides, the adaptor proteins FAM102A and FAM102B, and also N-BAR domain proteins at membrane-connected tubules. The absence of BLTP2 results in the accumulation of intracellular vacuoles, many of which are connected to the plasma membrane, pointing to a role of the lipid transport function of BLTP2 in the control of PM dynamics. - Source: PubMed
Publication date: 2025/02/08
Dai AnbangXu PengAmos ChaseFujise KenshiroWu YumeiYang HanEisen Julia NGuillén-Samander AndrésDe Camilli Pietro
Bioinformatics-based modeling of lung squamous cell carcinoma prognosis and prediction of immunotherapy response.
Lung squamous cell carcinoma (LUSC) is a subtype of non-small cell lung cancer. It has a grim prognosis for patients, primarily because the disease often remains asymptomatic in its early stages. As a result, it is frequently diagnosed at an advanced stage, limiting treatment options. This underscores the importance of studying potential biomarkers and developing personalized treatment strategies. In this study, we used an advanced bioinformatics approach, integrating two authoritative databases, NCBI's GEO and TCGA, to perform a large-scale cross-platform gene expression analysis. To deeply mine the gene expression data of a large number of lung squamous carcinoma samples, we used a screening strategy based on median absolute deviation to select genes that differed significantly in multiple datasets. The expression variations of these genes between normal and cancerous tissues provided us with valuable clues revealing key molecules that may be involved in the disease process. Through rigorous statistical tests, we identified 36 genes that were significantly associated with patient survival, and further constructed a model using Cox proportional risk model containing 11 key genes (MRPL40, GABPB1AS1, PTPN3, SNCA, PYGB, RAP1, VDR, PHPT1, KIAA0100, TBC1D30, CYP7B1) in a risk prediction model. The prediction model not only reflects the strong correlation between gene expression and LUSC prognosis, but also provides clinicians with an effective tool to predict patients' survival prospects. In the future, this model is expected to guide the development of individualized treatment plans, thereby improving the quality of life and overall prognosis of patients. - Source: PubMed
Publication date: 2024/12/26
Zhang QiqingHe HaidongWei YiLi GuopingShou Lu
Whole-exome sequencing of Nigerian benign prostatic hyperplasia reveals increased alterations in apoptotic pathways.
Through whole-exome sequencing of 60 formalin-fixed paraffin-embedded Nigerian (NGRn) benign prostatic hyperplasia (BPH) samples, we identified germline and somatic alterations in apoptotic pathways impacting BPH development and progression. Prostate enlargement is a common occurrence in male aging; however, this enlargement can lead to lower urinary tract symptoms that negatively impact quality of life. This impact is disproportionately present in men of African ancestry. BPH pathophysiology is poorly understood and studies examining non-European populations are lacking. - Source: PubMed
Publication date: 2024/01/08
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T101 DDH (Dihydrodiol Dehydrogenase)

Related genes to: T101 DDH (Dihydrodiol Dehydrogenase)

Related products to: T101 DDH (Dihydrodiol Dehydrogenase)

Related articles to: T101 DDH (Dihydrodiol Dehydrogenase)

BLTP2 bridges the ER and MVB for exosome biogenesis at SCAMP3-dependent ER contacts.

Multiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics.

Multiple interactions mediate the localization of BLTP2 at ER-PM contacts to control plasma membrane dynamics.

Bioinformatics-based modeling of lung squamous cell carcinoma prognosis and prediction of immunotherapy response.

Whole-exome sequencing of Nigerian benign prostatic hyperplasia reveals increased alterations in apoptotic pathways.