Polyclonal Rabbit BRSK1 Antibody
- Known as:
- Polyclonal Rabbit BRSK1 Antibody
- Catalog number:
- KA0452
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit BRSK1 Antibody
Related genes to: Polyclonal Rabbit BRSK1 Antibody
- Gene:
- BRSK1 NIH gene
- Name:
- BR serine/threonine kinase 1
- Previous symbol:
- -
- Synonyms:
- KIAA1811
- Chromosome:
- 19q13.42
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-12
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit BRSK1 Antibody
Related articles to: Polyclonal Rabbit BRSK1 Antibody
- We conducted a genome-wide calmodulin (CaM) interaction screening of 462 GST-fused human protein kinases to identify novel CaM-dependent protein kinases (CaMKs). In addition to known CaMKs, including myosin light chain kinases, CaMK2γ, and death-associated kinase 2, we identified the brain-specific protein kinase 2 (BRSK2, also known as SAD-A) as a novel CaM interactant. Proximity biotinylation and CaM-sepharose chromatography assays revealed that rat BRSK isoforms (BRSK1/2) interact with CaM in a Ca-dependent manner in vitro. We found that CaM suppresses the activation-loop phosphorylation of BRSK1 (at Thr189) and BRSK2 (at Thr175) by liver kinase B1 (LKB1), an activating kinase, in a Ca-dependent manner (IC of ∼7 µM), thereby inhibiting BRSK activation. LKB1-catalyzed phosphorylation of the catalytic domain mutant of BRSK1 (residues 1-294) at Thr189 was suppressed by the addition of Ca/CaM, consistent with direct CaM binding of the kinase domain, as well as wild-type BRSK1. We confirmed that the LKB1 activity was not directly suppressed by Ca/CaM, supporting the hypothesis that the direct interaction of Ca/CaM with the kinase domain blocks the phosphorylation/activation of BRSK1/2 by LKB1. The kinase activity and PP2Cα-catalyzed dephosphorylation of LKB1-phosphorylated BRSK1 were not altered by Ca/CaM, although it was demonstrated to bind to Ca/CaM like that of unphosphorylated BRSK1. This unrecognized mechanism of BRSK1/2 regulation, involving the direct role of Ca/CaM binding, which inhibits phosphorylation/activation by LKB1, may open a new Ca signal transduction pathway in neurons. - Source: PubMed
Publication date: 2026/03/20
Washida NaoyukiKataoka MoeBrun Anna RTakezaki UryuHijikawa KoYamauchi HarukiOhtsuka SatomiMagari MasakiMorishita RyoTokumitsu Hiroshi - Autism spectrum disorder (ASD) is a prevalent and complex neurodevelopmental disorder with a strong genetic basis. Although SH3RF3 has been identified as an ASD candidate gene, its biological function and pathophysiological mechanisms remain elusive. Here, we reveal that SH3RF3 functions as an essential scaffold protein that facilitates presynaptic vesicle docking. Mechanistically, it orchestrates the formation of a molecular complex between the kinase BRSK1/SAD-B and the ASD-associated active zone protein RIM1. Genetic ablation of Sh3rf3 disrupts this protein-protein interaction, leading to reduced RIM1 phosphorylation. This perturbation triggers synaptic dysfunctions, marked by a substantial reduction in both total synaptic vesicle (SV) density and readily releasable pool size, coupled with delayed SV replenishment kinetics. These deficits ultimately impair excitatory synaptic transmission in the prefrontal cortex, disturb the excitatory-inhibitory (E/I) balance, and elicit autistic-like behaviors in mice. Notably, prefrontal cortex-specific restoration of Sh3rf3 reverses behavioral and functional deficits in knockout mice. Furthermore, our characterization of the SH3RF3 interactome reveals a shared molecular network encompassing ASD-risk genes, indicating that synapse-targeted therapies may have broad applicability. - Source: PubMed
Publication date: 2025/11/25
Yuan YutingLi YangYang FuqiangJiang YishengDing YuanyuanXiao YingZhu XiliShu XingmeiHuang XiaheWang YingchunZhang ShuliSun JianyuanXu Zhiheng - Sorafenib is the first-line treatment agent for advanced hepatocellular carcinoma (HCC), but it is effective in very few patients. Thus, this study was intended to identify gene signatures associated with sorafenib response in HCC and construct a prognostic risk model based on these gene signatures. - Source: PubMed
Publication date: 2025/10/30
Zhao YuanyuDong JunfengZhong HanxiangPeng LiangxiWu LiangYu MeicenDing GuoshanGuo Wenyuan - The BRSK1 gene encodes brain-specific serine/threonine kinase 1 (also known as SAD-B kinase), which is almost exclusively expressed in the brain and plays critical roles in neuronal polarization, neurotransmitter release, mitochondrial dynamics, and neuronal maturation. This study aimed to investigate the pathogenicity of BRSK1 variants in epilepsy and neurodevelopmental disorders. - Source: PubMed
Publication date: 2025/10/02
Zhang QiYamanaka HiroshiLi PingLi YingfengLuo TianXia MiaoLiu TingLiu XueyanLu QingYang BinHe FanDu KaixianShu YoushengPeng BoJiang Yong-HuiWang Yi - Disruption of the Hippo pathway leads to activation of the YAP/TAZ transcriptional program which promotes tumor initiation, progression and metastasis in diverse cancers. Aggressive triple-negative breast cancers (TNBC) lack an effective therapy; thus, inactivating YAP and TAZ has emerged as an attractive approach and a new treatment modality. Thus, we performed two complementary high-throughput RNAi-based kinome screens to uncover cancer-associated activators of YAP/TAZ in two TNBC cell lines, MDA-MB231 and MDA-MB468. Integrated analysis that combined a YAP/TAZ localization screen with a TEAD-luciferase reporter screen, identified novel regulators including BRSK1, STK32C and STK40. The AMPK family members NUAKs, MARKs and SIKs are known to inhibit the Hippo kinase cassette; here, we uncover BRSK1, another AMPK family member as a regulator of YAP/TAZ. We also reveal that two poorly studied kinases, STK32C, a member of the AGC family, and STK40, a pseudokinase, can also inhibit the activity of YAP/TAZ. Thus, our studies expand the repertoire of known AMPK family members and reveal two new kinases that modulate the Hippo pathway and may play a role in YAP/TAZ driven breast cancers. Further analysis of other screen hits may similarly uncover new regulators that could be targeted for therapeutic interventions. - Source: PubMed
Publication date: 2025/08/13
Gill Mandeep KSong SiyuanChristova TaniaAttisano Liliana