h LARGE inducible lentiviral particles
- Known as:
- h LARGE inducible lentiviral beads
- Catalog number:
- LVP603
- Product Quantity:
- 1x107 IFU/ml x 200ul
- Category:
- -
- Supplier:
- GenTarget
- Gene target:
- LARGE inducible lentiviral particles
Related genes to: h LARGE inducible lentiviral particles
- Gene:
- LARGE1 NIH gene
- Name:
- LARGE xylosyl- and glucuronyltransferase 1
- Previous symbol:
- LARGE
- Synonyms:
- KIAA0609
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-02
- Date modifiied:
- 2019-04-23
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- Dystroglycan (DG) is an extracellular matrix receptor crucial for tissue development and pathogen entry. DG harbors a long, complex glycan called matriglycan. Loss of matriglycan or reduction in its length disrupts DG function, causing dystroglycanopathies. However, the mechanism regulating matriglycan length is unknown. In this study, we found that a xylose kinase facilitated the initiation of matriglycan synthesis by adding a phosphate to the xylose of the matriglycan primer. Matriglycan elongation occurred when the phosphate was removed by the N-terminal domain of DG (DGN). DGN has the conserved DXDXT/V active site motif found in haloacid dehalogenase domains of phosphohydrolases. Mutations in this site abolished DGN phosphatase activity, reduced matriglycan length, and caused muscle disease in mice. Thus, DG has an unexpected xylose phosphatase function involved in regulating matriglycan extension. - Source: PubMed
Publication date: 2026/08/13
Chandel IshitaVenzke DavidWollesen Bailey AYu LipingCampbell Kevin P - Glycosyltransferases often contain multiple structural modules that contribute to substrate recognition, catalytic coordination, and higher-order molecular organization. However, how multidomain glycosyltransferases dynamically organize their catalytic domains in solution remains poorly understood. Here, we investigated the assembly states and conformational dynamics of POMGNT2, LARGE1, K4CP, and L137 using high-speed atomic force microscopy (HS-AFM) integrated with complementary solution biophysical analyses. This multi-technique approach extends previous static structural studies by enabling a parallel comparison of solution-state dynamics among multiple glycosyltransferases. POMGNT2 formed a stable dimeric architecture with limited large-scale conformational fluctuation, consistent with its role in site-selective substrate recognition. In contrast, LARGE1 and K4CP exhibited concentration-dependent and heterogeneous assembly behavior. K4CP displayed pronounced open-closed interdomain motion and a tendency toward more compact conformations in the presence of substrate, suggesting dynamic catalytic-domain reorganization during glycan elongation. By comparison, the mimivirus glycosyltransferase candidate L137 predominantly behaved as a monomeric species under the tested conditions. These findings demonstrate that multidomain glycosyltransferases employ diverse dynamic organizational strategies ranging from rigid recognition architectures to highly flexible and reversible catalytic assemblies. Our results further suggest that glycosyltransferase function is governed not only by catalytic-domain structure, but also by dynamic conformational coordination adapted to distinct catalytic demands. - Source: PubMed
Publication date: 2026/07/19
Yagi HirokazuLin You-RongKanaoka YuiUmezawa FumikoKim AkemiTomuro KotaroMorishima KenKodama AtsujiIshii KentaroUchiyama SusumuSatoh TadashiSugiyama MasaakiUchihashi TakayukiKato Koichi - Diabetic peripheral neuropathy (DPN) is a common and disabling complication of diabetes for which no disease-modifying therapies are currently available. Glycemic and metabolic drivers do not fully explain why only a subset of individuals with diabetes develop DPN, and underling genetic contributors remain poorly defined. - Source: PubMed
Publication date: 2026/07/10
Fridman VeraKakar AasthaJensen AubreyVan de Vondel LiedeweiWheeler AllisonPhillips Lawrence SZhou JinZuchner StephanReusch JaneRaghavan Sridharan - α-Dystroglycan (α-DG) is a central component of the dystrophin-glycoprotein complex, with the characteristic O-mannosyl glycan modification, which binds to several extracellular matrix proteins such as laminin. Disruption in the synthesis of laminin-binding glycan on α-DG is related to muscular dystrophies. In addition, loss of this glycan is frequently observed in many cancers, including pancreatic ductal adenocarcinoma (PDAC), correlating with poor prognosis. However, the significance of this glycan in the pathology of cancer remains unclear. This study aimed to clarify the biological significance of laminin-binding O-mannosyl glycan on α-DG in PDAC cells. Since a tumor-derived cancer cell line consists of cells with diverse characteristics, we first obtained several single-cell-derived clones using MIA PaCa-2, a commonly used undifferentiated PDAC cell line, and found that the laminin-binding glycan modification level on α-DG differs among the various clones. The glycan modification level correlated well with the mRNA expression level of LARGE1, the enzyme that synthesizes the laminin-binding structure on the glycan. We analyzed several PDAC cell properties, such as cellular morphology, proliferation and migration/invasion abilities, and examined their correlation with the glycan modification. We found that a high level of laminin-binding O-mannosyl glycan modification on α-DG correlated with the elongated cell morphology, high invasion ability, and low membrane blebbing activity, and vice versa. Furthermore, manipulation of the laminin-binding O-mannosyl glycan synthesis confirmed that this glycan partially contributed to these properties. Overall, this study provides valuable insights into the roles of the laminin-binding glycan on α-DG in PDAC. - Source: PubMed
Publication date: 2026/01/16
Imae RiekoShichi YuukiNinagawa SatoshiIshiwata ToshiyukiManya Hiroshi - Grain size has long been recognized as a key determinant of yield potential in crops. Understanding the mechanisms governing grain size is critical for breeding high-yielding varieties. In a previous work, we revealed that the RNA-binding protein LARGE1 acts as a negative regulator of grain size and weight in rice. LARGE1 interacts with GSK2 (GLYCOGEN SYNTHASE KINASE2) and is phosphorylated by GSK2. Here, we report that LARGE1 physically interacts with an atypical non-DNA-binding bHLH protein PGL2 that positively influences grain size. Biochemical analyses show that PGL2 binds to APG, a typical DNA-binding bHLH protein that negatively regulates grain size. PGL2 suppresses the transcriptional activation activity of APG by forming the PGL2/APG heterodimer. Strikingly, LARGE1 can repress the formation of the heterodimer PGL2/APG by competitively binding PGL2, thereby releasing the inhibitory effect of PGL2 on the transcriptional activation activity of APG. Genetic evidence and RNA-seq analyses support that LARGE1 and PGL2 act in a common pathway to regulate grain size in rice. Our findings uncover a novel regulatory module GSK2-LARGE1-PGL2/APG that fine-tunes grain size, suggesting a promising target for improving seed size and weight in crops. - Source: PubMed
Liu YapeiZhang HaoGao YingXi XingniZhang YuhanLyu JiaZhang LiminLi Yunhai