Ask about this productRelated genes to: SYT5 antibody
- Gene:
- SYT5 NIH gene
- Name:
- synaptotagmin 5
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.42
- Locus Type:
- gene with protein product
- Date approved:
- 1995-09-27
- Date modifiied:
- 2015-11-20
Related products to: SYT5 antibody
Related articles to: SYT5 antibody
- PPP1R1A (protein phosphatase 1 regulatory inhibitor subunit 1A) is a cAMP/PKA-responsive inhibitor of protein phosphatase 1 (PP1) with a pivotal role in pancreatic β-cell physiology. To investigate its functional impact, Ppp1r1a was silenced in INS-1 (832/13) rat β-cells, and proteomic alterations were profiled using label-free DIA mass spectrometry (Orbitrap Exploris 480) with a rat spectral library. Quantitative analysis ( = 4/group) identified ∼2846 proteins with >2-fold change, revealing extensive proteome reprogramming. Key biological processes affected included vesicle trafficking and exocytosis, insulin biosynthesis and processing, organelle organization, mRNA processing, and autophagy. Pathway enrichment highlighted disruptions in insulin secretion, insulin resistance, and mTOR signaling. Crucial β-cell proteins, including INS2, Cacna1a, CPEB2, PCSK2, SNAP25, SYT5, and VAMP7, were significantly downregulated. Validation confirmed reduced phosphorylated AKT levels and p-AKT/T-AKT ratio, consistent with impaired mTOR signaling. Collectively, these findings demonstrate that PPP1R1A is essential for maintaining β-cell function and insulin secretion, and its depletion triggers broad proteomic and signaling alterations. Thus, PPP1R1A emerges as a regulatory node with potential therapeutic relevance in modulating β-cell activity and insulin dynamics in diabetes. - Source: PubMed
Publication date: 2025/12/08
Taneera JalalGiddey Alexander DSoares Nelson CKhalique AnilaMohammed Abdul KhaderMahgoub Mohamed OmerMahgoub Eglal - Hypoxic-ischemic encephalopathy (HIE) is a major cause of morbidity and mortality in newborns resulting in motor and cognitive impairment. Therapeutic hypothermia is the only treatment approved for HIE. Consequently, there is a critical requirement for additional treatments for hypoxic-ischemic (HI) brain injury because hypothermia is only partially protective. Pharmacological therapeutics are as yet not available to treat HIE. Therefore, we developed a novel trisubstituted purine-derivative drug (BRT_002) to attenuate HI related brain injury. The safety of BRT_002 was confirmed by treating adult rats with BRT_002 (100 mg/kg) for 7 days. Postnatal day-7 rats exposed to sham surgery or carotid ligation and 8% FiO for 90 min were given BRT_002 (30 mg/kg) or placebo intraperitoneally (IP) immediately, 24, and 48 h after the induction of HI. Pharmacokinetic studies revealed suitable systemic and brain exposure to BRT_002. Treatment with BRT_002 reduced neuropathological infarct volumes in the neonatal rats. Bioinformatics analyses of proteomic data identified upregulation of Agrin, Zyxin and Syt5 (p < 0.05) in both brain hemispheres in the male and female neonatal rats after treatment with BRT_002. BRT_002 also augmented mitochondrial respiration and produced metabolic changes in mouse neurons exposed to oxygen-glucose deprivation in vitro. Protein-protein interactions suggest that Syt5 interacts with major participants required to attenuate injury and/or facilitate parenchymal brain repair through Fblim1 that include Agrin, Zyxin, Vegfa, Vwf and mitochondrial targets. Our study provides preclinical findings that could serve as a foundation for future clinical trials of this novel purine derivative for the treatment of newborns exposed to HIE. - Source: PubMed
Publication date: 2025/06/17
Mabondzo AloïseDisdier ClémenceBouzid AmalLarbi Khadidja SideTsintzou AmaliaMaïza AurianeKim BoramCosta NarcisoHarati RaniaNguyen Anvi LaetitiaPruvost AlainGalons HervéOumata NassimaArmengaud JeanKnijnenburg MarlouVerma GauravHagberg HenrikGressens PierreChen Xiaodi FHamoudi Rifat AStonestreet Barbara S - Macroautophagy/autophagy progresses through Ca-dependent multiple fusion events. Recently, we reported that the intracellular Ca channel MCOLN3/TRPML3 provides Ca for membrane fusion during autophagosome formation as a downstream effector of phosphatidylinositol-3-phosphate (PtdIns3P). However, the molecular mechanism of Ca signaling in the late stage of autophagy remains unknown. Here, we show that the MCOLN1/TRPML1-MCOLN3/TRPML3 heteromer is the Ca provider for autophagosome-lysosome fusion. MCOLN1-MCOLN3 functions downstream of PtdIns4P to release Ca from autophagosomes, and the Ca signal via PtdIns4P-MCOLN1-MCOLN3 is decoded by the Ca sensor SYT5 (synaptotagmin 5). The binding of Ca and PtdIns4P to SYT5 is critical for autophagosome-lysosome fusion by forming a fusion complex. Collectively, these results reveal that PtdIns4P-MCOLN1-MCOLN3-SYT5 constitutes the Ca signaling complex in autophagosome-lysosome fusion and that MCOLN3 also regulates the late stage of autophagy through heteromerization with MCOLN1 in a phosphoinositide (PI)-dependent manner.: ATG, autophagy related; CPA, cyclopiazonic acid; DN, dominant-negative; GPN, glycyl-L-phenylalanine-beta-naphthylamide; KO, knockout; NHCl, ammonium chloride; PtdIns3K, phosphatidylinositol 3-kinase; PtdIns3P, phosphatidylinositol-3-phosphate; PI, phosphoinositide; SYT5, synaptotagmin 5; tfLC3, mRFP-GFP tandem fluorescent-tagged LC3; WT, wild-type. - Source: PubMed
Publication date: 2025/05/27
Kwon JinKim So WoonHong SeokwooChoi AreumChoi SuziPark Myoung KyuKim Hyun Jin - Identification of those at high and low risk of disease relapse is a major unmet need in the management of patients with ANCA-associated vasculitis (AAV). Precise stratification would allow tailoring of immunosuppressive medication. We profiled the autoantibody repertoire of AAV patients in remission to identify novel autoantibodies associated with relapse risk. - Source: PubMed
Bayati ShaghayeghNazeer JamsheelaNg JamesGeorge Angel MHayes MichaelLittle Mark ANilsson PeterPin Elisa - Endoplasmic reticulum-plasma membrane contact sites (ER-PM CSs) are evolutionarily conserved membrane domains found in all eukaryotes, where the ER closely interfaces with the PM. This short distance is achieved in plants through the action of tether proteins such as synaptotagmins (SYTs). Arabidopsis comprises five SYT members (SYT1-SYT5), but whether they possess overlapping or distinct biological functions remains elusive. SYT1, the best-characterized member, plays an essential role in the resistance to abiotic stress. This study reveals that the functionally redundant SYT1 and SYT3 genes, but not SYT5, are involved in salt and cold stress resistance. We also show that, unlike SYT5, SYT1 and SYT3 are not required for Pseudomonas syringae resistance. Since SYT1 and SYT5 interact in vivo via their SMP domains, the distinct functions of these proteins cannot be caused by differences in their localization. Interestingly, structural phylogenetic analysis indicates that the SYT1 and SYT5 clades emerged early in the evolution of land plants. We also show that the SYT1 and SYT5 clades exhibit different structural features in their SMP and Cabinding of their C2 domains, rationalizing their distinct biological roles. - Source: PubMed
Publication date: 2024/09/10
García-Hernández SeleneRubio LourdesRivera-Moreno MaríaPérez-Sancho JessicaMorello-López JorgeEsteban Del Valle AliciaBenítez-Fuente FranciscoBeuzón Carmen RMacho Alberto PRuiz-López NoemiAlbert ArmandoBotella Miguel A