TULP3 antibody - middle region (ARP33473_P050)
- Known as:
- TULP3 (anti-) - middle region (ARP33473_P050)
- Catalog number:
- arp33473_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TULP3 antibody - middle region (ARP33473_P050)
Related genes to: TULP3 antibody - middle region (ARP33473_P050)
- Gene:
- TULP3 NIH gene
- Name:
- TUB like protein 3
- Previous symbol:
- -
- Synonyms:
- TUBL3
- Chromosome:
- 12p13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-11
- Date modifiied:
- 2019-04-11
Related products to: TULP3 antibody - middle region (ARP33473_P050)
Related articles to: TULP3 antibody - middle region (ARP33473_P050)
- Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are mainstay therapies for diabetes and obesity, acting in part by enhancing glucose-dependent insulin secretion. While the primary cilium is a known signaling compartment for certain G-protein coupled receptors (GPCRs), its role in the β-cell response to incretins remains undefined. Here, we show that primary cilia are essential for full GLP-1R signaling. Loss of β-cell cilia in mouse and human islets severely impaired GLP-1-potentiated insulin secretion, an effect preceded by blunted whole-cell cAMP and Ca responses. Immunofluorescence and immunogold scanning electron microscopy revealed endogenous GLP-1R localized to the primary cilium. Adenylyl cyclase immunostaining was also enriched within cilia, and targeted inhibition of ciliary PKA reduced insulin secretion. Critically, disrupting ciliary GPCR trafficking via Tulp3 knockdown - while preserving cilia structure - recapitulated the signaling and secretory deficits, demonstrating a specific requirement for the ciliary receptor pool. These findings establish the primary cilium as a non-redundant signaling compartment for GLP-1R and uncover a new layer of subcellular organization in incretin action in β cells. - Source: PubMed
Publication date: 2026/03/25
Melena IsabellaJo Jeong HunTownsend Shannon EDiGruccio Samantha AdamsonDong XinhangZhu LifeiCampbell JonathanHughes Jing W - Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are mainstay therapies for diabetes and obesity, acting in part by enhancing glucose-dependent insulin secretion. While the primary cilium is a known signaling compartment for certain G-protein coupled receptors (GPCRs), its role in the β-cell response to incretins remains undefined. Here, we show that primary cilia are essential for GLP-1R signaling. Loss of β-cell cilia in mouse and human islets severely impaired GLP-1-potentiated insulin secretion, an effect preceded by blunted whole-cell cAMP and Ca²⁺ responses. Immunofluorescence and immunogold scanning electron microscopy revealed endogenous GLP-1R localized to the primary cilium. Critically, disrupting ciliary GPCR trafficking via Tulp3 knockdown - while preserving cilia structure - recapitulated the signaling and secretory deficits, demonstrating a specific requirement for the ciliary receptor pool. These findings establish the primary cilium as a non-redundant signaling compartment for GLP-1R and uncover a new layer of subcellular organization in incretin action in β cells. - Source: PubMed
Publication date: 2026/02/22
Melena IsabellaJo Jeong HunTownsend Shannon EDiGruccio Samantha AdamsonDong XinhangZhu LifeiCampbell JonathanHughes Jing W - A HaloTag knock-in resource allows direct visualization of endogenous polycystin-2 (PC2), enabling quantitative analysis of its localization, turnover, and transport dynamics. PC2-HaloTag labeling establishes PC1-dependent and Tulp3-dependent control of PC2 ciliary targeting in vivo and in cells. - Source: PubMed
Publication date: 2026/02/10
Li ZhangHaycraft Courtney JCroyle Mandy JHudson DanielYuan YuanSimanyi KristinVendrame Hanan ChweihWang JunKachwala Alfiya IbrahimbhaiMa YongjieParant John MChumley PhillipZhou JulingMrug MichalParnell Stephen CTran Pamela VGao HongjuanQian FengOuteda PatriciaWallace Darren PWatnick Terry JYoder Bradley K - - Source: PubMed
Publication date: 2026/01/12
Epting DanielDevane JohnMertes RalfKayser SéverineHelmstädter MartinMetzger PatrickBoerries MelanieBergmann CarstenOtt Elisabeth - My independent career started based on a simple doctrine of protein multifunctionality, by intuitively choosing the protein called AXIN, which has turned out to be the protagonist of my scientific life. This led us to discover the sensing pathway for glucose, which links to AMPK and mTORC1, two master metabolic controllers. We found that AXIN binds LKB1, an upstream kinase of AMPK, and that the AXIN:LKB1 complex translocates to the lysosomal surface after the lysosomal aldolase senses low glucose (fructose-1,6-bisphosphate as the direct signal) to activate AMPK and concomitantly inhibit mTORC1. Remarkably, we found that the lysosomal glucose-sensing AMPK pathway is shared by metformin, a glucose-lowering drug known to also extend lifespan and reduce cancer risk. In search of metabolites enriched in calorie-restricted mice and able to activate AMPK via the lysosomal pathway, we identified that lithocholic acid (LCA) as such a factor. We also identified TULP3 as the LCA receptor, which signals to activate sirtuins, increase NAD, activate AMPK and inhibit mTORC1. In translation, we have identified an aldolase inhibitor termed aldometanib, which mimics glucose starvation to activate AMPK. Aldometanib can alleviate fatty liver, lower blood glucose, and extend lifespan in animals. Surprisingly, aldometanib can also mobilize tumoricidal CD8 T cells to infiltrate and contain hepatocellular carcinomas (HCC), enabling HCC-bearing mice to live to ripe ages, the endpoint of cancer therapy. Our work has thus revealed that glucose acts as a messenger that signals through a specialized route to control health-span and lifespan. We will continue to explore the teleological meaning of glucose as a "chosen" molecule. - Source: PubMed
Publication date: 2026/01/09
Lin Sheng-Cai