Ask about this productRelated genes to: LDB1 antibody
- Gene:
- LDB1 NIH gene
- Name:
- LIM domain binding 1
- Previous symbol:
- -
- Synonyms:
- NLI, CLIM2
- Chromosome:
- 10q24.32
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-22
- Date modifiied:
- 2016-10-05
- Gene:
- LDB2 NIH gene
- Name:
- LIM domain binding 2
- Previous symbol:
- -
- Synonyms:
- CLIM1, LDB1
- Chromosome:
- 4p15.32
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-22
- Date modifiied:
- 2016-10-05
Related products to: LDB1 antibody
Related articles to: LDB1 antibody
- Over the past few years, significant investments in smart traffic monitoring systems have been made. The most important step in machine learning is detecting and recognizing objects relative to vehicles. Due to variations in vision and different lighting conditions, the recognition and tracking of vehicles under varying extreme conditions has become one of the most challenging tasks. To deal with this, our proposed system presents an adaptive method for robustly recognizing several existing automobiles in dense traffic settings. Additionally, this research presents a broad framework for effective on-road vehicle recognition and detection. Furthermore, the proposed system focuses on challenges typically noticed in analyzing traffic scenes captured by in-vehicle cameras, such as consistent extraction of features. First, we performed frame conversion, background subtraction, and object shape optimization as preprocessing steps. Next, two important features (energy and deep optical flow) were extracted. The incorporation of energy and dense optical flow features in distance-adaptive window areas and subsequent processing over the fused features resulted in a greater capacity for discrimination. Next, a graph-mining-based approach was applied to select optimal features. Finally, the artificial neural network was adopted for detection and classification. The experimental results show significant performance in two benchmark datasets, including the LISA and KITTI 7 databases. The LISA dataset achieved a mean recognition rate of 93.75% on the LDB1 and LDB2 databases, whereas KITTI attained 82.85% accuracy on separate training of ANN. - Source: PubMed
Publication date: 2023/02/03
Wieczorek GrzegorzTahir Sheikh Badar Ud DinAkhter IsrarKurek Jaroslaw - The Lim domain binding proteins (LDB1 and LDB2 in human and Chip in ) play critical roles in cell fate decisions through partnership with multiple Lim-homeobox and Lim-only proteins in diverse developmental systems including cardiogenesis, neurogenesis, and hematopoiesis. In mammalian erythroid cells, LDB1 dimerization supports long-range connections between enhancers and genes involved in erythropoiesis, including the β-globin genes. Single-stranded DNA binding proteins (SSBPs) interact specifically with the LDB/Chip conserved domain (LCCD) of LDB proteins and stabilize LDBs by preventing their proteasomal degradation, thus promoting their functions in gene regulation. The structural basis for LDB1 self-interaction and interface with SSBPs is unclear. Here we report a crystal structure of the human LDB1/SSBP2 complex at 2.8-Å resolution. The LDB1 dimerization domain (DD) contains an N-terminal nuclear transport factor 2 (NTF2)-like subdomain and a small helix 4-helix 5 subdomain, which together form the LDB1 dimerization interface. The 2 LCCDs in the symmetric LDB1 dimer flank the core DDs, with each LCCD forming extensive interactions with an SSBP2 dimer. The conserved linker between LDB1 DD and LCCD covers a potential ligand-binding pocket of the LDB1 NTF2-like subdomain and may serve as a regulatory site for LDB1 structure and function. Our structural and biochemical data provide a much-anticipated structural basis for understanding how LDB1 and the LDB1/SSBP interactions form the structural core of diverse complexes mediating cell choice decisions and long-range enhancer-promoter interactions. - Source: PubMed
Publication date: 2019/12/31
Wang HongyangKim JuhyunWang ZhizhiYan Xiao-XueDean AnnXu Wenqing - The Chip/LIM-domain binding protein (LDB)-single-stranded DNA-binding protein (SSDP) (ChiLS) complex controls numerous cell-fate decisions in animal cells, by mediating transcription of developmental control genes via remote enhancers. ChiLS is recruited to these enhancers by lineage-specific LIM-domain proteins that bind to its Chip/LDB subunit. ChiLS recently emerged as the core module of the Wnt enhanceosome, a multiprotein complex that primes developmental control genes for timely Wnt responses. ChiLS binds to NPFxD motifs within Pygopus (Pygo) and the Osa/ARID1A subunit of the BAF chromatin remodeling complex, which could synergize with LIM proteins in tethering ChiLS to enhancers. Chip/LDB and SSDP both contain N-terminal dimerization domains that constitute the bulk of their structured cores. Here, we report the crystal structures of these dimerization domains, in part aided by DARPin chaperones. We conducted systematic surface scanning by structure-designed mutations, followed by in vitro and in vivo binding assays, to determine conserved surface residues required for binding between Chip/LDB, SSDP, and Pygo-NPFxD. Based on this, and on the 4:2 (SSDP-Chip/LDB) stoichiometry of ChiLS, we derive a highly constrained structural model for this complex, which adopts a rotationally symmetrical SSDP-LDB-SSDP architecture. Integrity of ChiLS is essential for Pygo binding, and our mutational analysis places the NPFxD pockets on either side of the Chip/LDB dimer, each flanked by an SSDP dimer. The symmetry and multivalency of ChiLS underpin its function as an enhancer module integrating Wnt signals with lineage-specific factors to operate context-dependent transcriptional switches that are pivotal for normal development and cancer. - Source: PubMed
Publication date: 2019/09/30
Renko MihaFiedler MarcRutherford Trevor JSchaefer Jonas VPlückthun AndreasBienz Mariann - The Lim domain-binding proteins are key co-factor proteins that assemble with LIM domains of the LMO/LIM-HD family to form functional complexes that regulate cell proliferation and differentiation. Using conditional mutagenesis and comparative phenotypic analysis, we analyze the function of Ldb1 and Ldb2 in mouse retinal development, and demonstrate overlapping and specific functions of both proteins. Ldb1 interacts with Lhx2 in the embryonic retina and both Ldb1 and Ldb2 play a key role in maintaining the pool of retinal progenitor cells. This is accomplished by controlling the expression of the Vsx2 and Rax, and components of the Notch and Hedgehog signaling pathways. Furthermore, the Ldb1/Ldb2-mediated complex is essential for generation of early-born photoreceptors through the regulation of Rax and Crx. Finally, we demonstrate functional redundancy between Ldb1 and Ldb2. Ldb1 can fully compensate the loss of Ldb2 during all phases of retinal development, whereas Ldb2 alone is sufficient to sustain activity of Lhx2 in both early- and late-stage RPCs and in Müller glia. By contrast, loss of Ldb1 disrupts activity of the LIM domain factors in neuronal precursors. An intricate regulatory network exists that is mediated by Ldb1 and Ldb2, and promotes RPC proliferation and multipotency; it also controls specification of mammalian retina cells. - Source: PubMed
Publication date: 2016/10/03
Gueta KerenDavid AhuvitCohen TsadokMenuchin-Lasowski YotamNobel HilaNarkis GinatLi LiQiLove Paulde Melo JimmyBlackshaw SethWestphal HeinerAshery-Padan Ruth - Cofactors of LIM domain proteins, CLIM1 and CLIM2, are widely expressed transcriptional cofactors that are recruited to gene regulatory regions by DNA-binding proteins, including LIM domain transcription factors. In the cornea, epithelium-specific expression of a dominant negative (DN) CLIM under the keratin 14 (K14) promoter causes blistering, wounding, inflammation, epithelial hyperplasia, and neovascularization followed by epithelial thinning and subsequent epidermal-like differentiation of the corneal epithelium. The defects in corneal epithelial differentiation and cell fate determination suggest that CLIM may regulate corneal progenitor cells and the transition to differentiation. Consistent with this notion, the K14-DN-Clim corneal epithelium first exhibits increased proliferation followed by fewer progenitor cells with decreased proliferative potential. In vivo ChIP-sequencing experiments with corneal epithelium show that CLIM binds to and regulates numerous genes involved in cell adhesion and proliferation, including limbally enriched genes. Intriguingly, CLIM associates primarily with non-LIM homeodomain motifs in corneal epithelial cells, including that of estrogen receptor α. Among CLIM targets is the noncoding RNA H19 whose deregulation is associated with Silver-Russell and Beckwith-Wiedemann syndromes. We demonstrate here that H19 negatively regulates corneal epithelial proliferation. In addition to cell cycle regulators, H19 affects the expression of multiple cell adhesion genes. CLIM interacts with estrogen receptor α at the H19 locus, potentially explaining the higher expression of H19 in female than male corneas. Together, our results demonstrate an important role for CLIM in regulating the proliferative potential of corneal epithelial progenitors and identify CLIM downstream target H19 as a regulator of corneal epithelial proliferation and adhesion. - Source: PubMed
Publication date: 2016/04/29
Klein Rachel HerndonStephens Denise NHo HsiangChen Jefferson KSalmans Michael LWang WinnieYu ZhengquanAndersen Bogi