Ask about this productRelated genes to: BIN2 Blocking Peptide
- Gene:
- BIN2 NIH gene
- Name:
- bridging integrator 2
- Previous symbol:
- -
- Synonyms:
- BRAP-1
- Chromosome:
- 12q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-25
- Date modifiied:
- 2016-04-25
Related products to: BIN2 Blocking Peptide
Related articles to: BIN2 Blocking Peptide
- Brassinosteroids (BRs) are plant steroid hormones sensed by the membrane receptor kinase BRI1. Activation of BRI1 leads to the dephosphorylation of BZR1/BES1 transcription factors. Overexpression of the Kelch phosphatase BRI1 SUPPRESSOR 1 (BSU1) rescued the growth defects of mutants. Subsequent studies identified BSU1 as a protein tyrosine phosphatase, which promotes BR signaling by dephosphorylating a phosphotyrosine in the glycogen synthase kinase 3 BIN2. Crystal structures of the BSU1 phosphatase domain now reveal a high degree of structural similarity to protein phosphatase 1 (PP1), a eukaryotic serine/threonine phosphatase. Consistently, BSU1 efficiently dephosphorylated phosphothreonine- and phosphoserine-containing substrate peptides, but showed no detectable activity toward BIN2 and other phosphotyrosine substrates. A catalytically inactive BSU1 phosphatase domain suppresses the growth phenotypes of the Arabidopsis mutant and binds the BSU1 homologs BSL1-3. and loss-of-function mutants display wild-type-like BR responses, but exhibit stomatal patterning and fertility defects. Importantly, the PP1-like C-terminal tail of BSU1 is phosphorylated at Thr785 by a cyclin-dependent kinase complex. The phosphorylated tail binds to the BSU1 substrate-binding grooves, blocking access to the active site. Mutation of Thr785 to alanine activates BSU1, suggesting that Kelch phosphatases and PP1 share a common regulatory mechanism. Deletion of the Kelch phosphatase MpBSLM results in an undifferentiated cell mass phenotype, associated with the overactivation of a cell cycle reporter. Taken together, our experiments suggest that plant Kelch phosphatases act as PP1-like cell cycle regulators, rather than as tyrosine phosphatases in BR signaling. - Source: PubMed
Publication date: 2026/05/20
Rico-Resendiz FelixPri-Tal OdedRaia PierreMoretti AndreaChen HoumingYu JunBroger LarissaFuchs ChristelleHothorn Ludwig ALoubéry SylvainHothorn Michael - In laboratory-based diffraction contrast tomography (LabDCT), pixel binning on 2D detectors is an effective strategy to reduce exposure time and improve acquisition efficiency. However, its impact on reconstruction accuracy remains unclear. To address this, we systematically compared LabDCT datasets acquired without detector binning and with 2 × 2 binning, using synchrotron-based DCT (SRDCT) as the ground truth reference. The results show that unbinned (bin1) acquisitions yield higher grain indexing rates and improved grain boundary position accuracy compared with binned data (bin2), particularly for small grains near the sample surface. This improvement is attributed to the longer exposure time, finer spatial sampling (i.e. smaller effective pixel size), and a lower effective detection-size threshold during spot segmentation. To mitigate the information loss induced by binning, we employed a deep-learning spot-segmentation model (Mask R-CNN), which substantially improves reconstructions from binned images and narrows the performance gap relative to unbinned data. Finally, guidelines for further optimization of LabDCT acquisition and reconstruction are proposed. - Source: PubMed
Publication date: 2026/04/19
Ni XinboXia YipingFang HaixingLu JiayiLin FengxiangFan GuohuaZhang Yubin - Root developmental plasticity enables plants to adapt to nutrient-deficient conditions. Under low-nitrate (LN) conditions, enhanced exploratory root growth-characterized by increased primary and lateral root (LR) elongation-facilitates nutrient foraging. Although nitrate-hormone crosstalk regulates this process, the underlying molecular mechanisms remain poorly understood. Here, we identify the BIN2-GRF5-UBP12/13 module that governs root foraging responses to LN in Arabidopsis. We demonstrate that BIN2 phosphorylates GRF5 at Ser205, thereby reducing its stability and transcriptional activity. Integrative DAP-seq and transcriptomic analyses reveal that GRF5 directly regulates key nitrate-responsive genes, including the dual-affinity transporter gene NRT1.1 and the high-affinity uptake gene NRT2.1. Furthermore, dephosphorylated GRF5 preferentially interacts with UBIQUITIN-SPECIFIC PROTEASES 12 and 13 (UBP12/13), which stabilizes GRF5 and promotes LR elongation under LN conditions. Our findings delineate a phosphorylation-dependent regulatory circuit that fine-tunes root foraging adaptation, advancing the mechanistic understanding of nitrate sensing in plants. - Source: PubMed
Publication date: 2026/04/27
Li TaotaoYao XiuhongLiu DongxiaoKang XinkeFang KeZhao MeiZhao YuqingCai YueliSun JingjingTian WenhuiGong LupingWu ZhenjiangWei WenxiLi MengyuanLiao ChunliWang LianzheLin HonghuiZhang Dawei - Parental contributions to offspring phenotype extend beyond genetic inheritance, encompassing non-genetic factors that influence early development. However, the interplay between maternal and paternal effects remains poorly understood. This study investigates these contributions in Eurasian perch (Perca fluviatilis) - a valuable model to study parental effect in finfishes - by analyzing early life traits and transcriptomic profiles of larvae resulting from crosses between wild and domesticated parents. - Source: PubMed
Publication date: 2026/04/20
Debernardis RossellaPanda AbhipsaWałdowska SylwiaPalińska-Żarska KatarzynaKlopp Christophede Almeida Taina RochaJarmołowicz SylwiaHliwa PiotrŻarski Daniel - There is accumulating evidence suggesting an association between periodontitis (PD) and preterm birth (PTB), but the underlying mechanisms have not been fully elucidated. This study aims to explore potential biomarkers and mechanisms between PD and PTB through integrated bioinformatics and machine learning approaches. - Source: PubMed
Publication date: 2026/02/20
Mei FengLiu YutongXu WentingLiu RuoyunWang XinlinLi TingtingChen YiWu TingtingZhang Wei