Ask about this productRelated genes to: BIN2 antibody
- 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 antibody
Related articles to: BIN2 antibody
- Guard cell movement is orchestrated by complex internal and environmental signals, with ZmGCT1 and ZmGCT2 playing critical roles in maintaining guard cell turgor in maize. Here, we demonstrate that ZmGCT1 interacts with and inhibits ZmSK4, a GSK3-like kinase. Under drought stress, ABA-activated ZmSnRK2s phosphorylate ZmGCT1, relieving its partial inhibition of ZmSK4, which, together with the relief of ZmPP2Cs-mediated inhibition, leads to ZmSK4 activation. ZmSK4 directly phosphorylates ZmSLAC1 and activates its anion currents in Xenopus oocytes, which ultimately promotes stomatal closure under drought stress. Consistent with this mechanism, mutations in ZmSK4 and its homolog ZmSK3 not only confer drought sensitivity but also suppress the constitutively closed stomata phenotype of the Zmgct1 mutant. Notably, in contrast to its BIN2 homologs, which do not regulate stomatal movement in Arabidopsis but stomatal development, ZmSK4 and ZmSK3 do not influence stomatal development in maize. Our findings thus delineate a complete phosphorylation relay within the ABA signaling pathway that dynamically regulates stomatal movement under drought stress in maize. - Source: PubMed
Publication date: 2026/07/14
Li HuiyingFeng ZhenkaiCheng JinkuiWang YuQi JunshenSong WenYang ShuhuaGong Zhizhong - Plant glycogen synthase kinase 3 (GSK3) integrates development and environment. Unlike animals, plants have expanded this family: Arabidopsis has ten GSK3s and rice has nine. BIN2 was once seen as just a brake for brassinosteroid (BR) signaling. That view is now outdated. Four paradigms now define GSK3 function: (1) bidirectional regulation - it both destabilizes and stabilizes substrates; (2) multimodal control - phosphorylation, acetylation, oxidation, S-nitrosylation, and ubiquitination-dependent turnover; (3) subcellular localization as a functional switch; (4) direct application in crop improvement. We examine how GSK3 activity, stability, and localization are controlled, and propose an integrated model: a "modification code", protein abundance, localization, and non-covalent interactions together determine functional output. We also discuss how GSK3 interacts with its structural context and the cellular environment. Finally, we translate these findings into strategies for crop improvement, including species-specific modulation of this conserved growth regulator, divergent stress responses, and three precision engineering strategies: phosphosite editing, tissue-specific knockdown, and scaffold targeting. Our goal is to move from static gene catalogs to mechanistic frameworks and to provide a roadmap for harnessing GSK3 pleiotropy in trait-specific crop improvement. - Source: PubMed
Publication date: 2026/07/10
Wang LianzheSong YiweiLin DaocongLi Taotao - DNA replication stress poses a severe threat to genome stability. It is well-known that SOG1 plays a crucial role in DNA replication stress response in plants. Although ATM-mediated phosphorylation and CRL4-mediated polyubiquitination of SOG1 play important roles in regulating DNA damage response (DDR), the posttranslational modifications of SOG1 during the replication stress response are little known. Here we show that, during replication stress, the activity of the GSK3-like kinase BIN2 is activated by an unknown mechanism independent of ATR. Subsequently, BIN2 phosphorylates SOG1 at T244 and T249, which enhances SOG1 stability and transcriptional activity to activate DDR. Thus, our study demonstrated a pathway by which plants dynamically regulate replication stress response by a BIN2-SOG1 module. - Source: PubMed
Publication date: 2026/07/03
Zhang JieGuo DongbeiZhang YifanWei FanHan QingLao JiahongWang HanFeng MenglingLuo XiruiWang ChaoLin HonghuiZhang Dawei - : ASD is a class of neurodevelopmental disorders with onset in early childhood, whereas AD is a common chronic inflammatory skin disease. An increasing number of studies suggest that immune dysregulation and inflammatory responses play important roles in the onset and progression of both conditions; however, their shared molecular mechanisms remain unclear. : First, ASD-related and AD-related datasets were obtained from the GEO database. After removal of batch effects, the common DEGs between the two diseases were identified. Subsequently, 107 machine learning-based model configurations were employed to screen for key genes. Functional enrichment analyses and PPI network construction were performed to systematically explore their potential functions. Finally, the CIBERSORT was applied to analyze immune cell infiltration and to assess the correlation between hub gene expression and immune cell infiltration. : 164 common genes between ASD and AD were identified. GO and KEGG enrichment analyses revealed that these shared differentially expressed genes were mainly enriched in pathways related to immune regulation and inflammatory responses, suggesting that immuno-inflammatory processes may constitute an important biological basis linking ASD and AD. Further screening and validation using machine learning identified , , , , , , and as hub genes serving as common potential biomarkers for both diseases. Among them, , , and may represent key shared genes and demonstrated good diagnostic value in ROC curve and nomogram analyses. In addition, immune infiltration analysis indicated that these key genes were significantly correlated with the infiltration levels of multiple immune cell types, further supporting their potential roles in immune regulation. : This study reveals potential shared immuno-inflammatory molecular mechanisms between ASD and AD. Genes screened based on 107 machine learning models were verified as potential diagnostic biomarkers for both diseases after integrated analysis, providing a theoretical basis for further investigation of their immune-related pathogenesis and early clinical diagnosis. - Source: PubMed
Publication date: 2026/05/12
Yang RuilingZhang FushenHuang Jufang - 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