Ask about this productRelated genes to: CAV1 Blocking Peptide
- Gene:
- CAV1 NIH gene
- Name:
- caveolin 1
- Previous symbol:
- CAV
- Synonyms:
- -
- Chromosome:
- 7q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-02
- Date modifiied:
- 2016-10-05
Related products to: CAV1 Blocking Peptide
Related articles to: CAV1 Blocking Peptide
- African swine fever virus (ASFV) poses a severe threat to the global pig industry, yet the precise mechanisms of its entry into host cells are not fully understood. In this study, we identified the host ribosomal protein SA (RPSA), a protein located in lipid rafts, as a critical viral receptor that facilitates ASFV entry. Immunoprecipitation-mass spectrometry (IP-MS) screening results identified RPSA as a binding partner of the ASFV capsid protein pE120R, which was further confirmed by co-immunoprecipitation (Co-IP) and immunofluorescence assays (IFA) in ASFV-infected cells. Moreover, knockdown of RPSA expression in porcine alveolar macrophages (PAMs) by siRNA significantly reduced ASFV attachment and internalization. In contrast, ectopic overexpression of RPSA in permissive CV-1 cells enhanced the attachment and internalization of ASFV virions. Additionally, we observed that both pharmacological inhibition of caveola-mediated endocytosis (CavME) with nystatin and genetic knockdown of caveolin-1 (CAV1) decreased caveola-mediated ASFV virions endocytosis and internalization. Mechanistically, RPSA interacts with CAV1, a major structural protein of caveolae. Domain mapping showed that pE120R mainly binds to the LR2 and LR3 domains of RPSA, while RPSA interacts with CAV1 via its 16B domain, forming a pE120R-RPSA-CAV1 complex that facilitates ASFV entry. Overall, these results demonstrate that RPSA works as a potential host receptor linking ASFV pE120R to the CAV1-mediated endocytic pathway, facilitating viral entry through caveola-mediated endocytosis. These findings advance our understanding of ASFV entry mechanism and offer a potential target for antiviral strategies against ASFV. - Source: PubMed
Publication date: 2026/05/11
Liu ChuanxiaLi TingtingWang YibingZhao FeiLi JiangnanHuang LiWeng Changjiang - Acute kidney injury (AKI) is a severe clinical condition with high morbidity and mortality. Caveolin-1 (Cav-1), a main structural protein of caveolae, orchestrates key cellular processes including endocytosis, lipid transport, and signal transduction by serving as a platform. However, its specific role in AKI remains unclear. Here, we report that Cav-1 is upregulated in distal tubule epithelial cells (TECs) in both AKI patients and mouse models induced by ischemia/reperfusion injury (IRI) and lipopolysaccharide (LPS). Global and distal TEC-specific Cav1 knockout exacerbates IRI and LPS-induced AKI. RNA-seq reveals that Cav-1 deficiency exacerbates intracellular calcium ion (Ca) homeostasis imbalance and endoplasmic reticulum (ER) stress in injured kidney tissues. Mechanistically, Cav-1 interacts with sarcoplasmic/endoplasmic reticulum Ca-ATPase 2 (SERCA2), a key regulator of intracellular Ca homeostasis, through its scaffolding domain, promoting SERCA2 deubiquitination and stability in the ER, thereby maintaining intracellular Ca homeostasis and suppressing ER stress in distal TECs. Furthermore, supplementation with a cell-permeable Cav-1 scaffolding domain peptide (CSP) or activation of SERCA2 with a small-molecule agonist CDN1163 alleviates IRI- and LPS-induced AKI, while distal TEC-specific SERCA2 knockdown abrogates CSP's therapeutic effect. Together, these findings reveal a novel Cav-1-mediated pathway and highlight its potential as a therapeutic target for AKI. - Source: PubMed
Publication date: 2026/05/08
Zhang YanHe XinHuang HaoLu RongLv XinLi ShenglanZou SijueCheng JiaweiXiong YiweiDeng ZhenghaoYuan QiongjingXie YanyunHuang LingPu JiaxiLiu ShaoLi QianbinMeng JieYang HuixiangTao LijianPeng Zhangzhe - Caveolin-1 (Cav-1) is a membrane-associated scaffolding protein essential for lipid regulation, cellular signaling, and caveolae formation. Phosphorylation at tyrosine 14 (Y14) of Cav-1 plays a pivotal role in modulating its functional dynamics, but the structural consequences of this modification remain unexplored. This site belongs to the N-terminal tail, which is unresolved in the recent CryoEM structures of the Cav-1 8S complexes. In this work, we used AlphaFold 3 to generate a full-length model of the human Cav-1 8S complex and its phosphorylated form (pCav-1) and performed molecular dynamics simulations of both complexes embedded in the plasma membrane. Inclusion of the N-terminal tail in the AF3-predicted models significantly enhances protein-membrane interactions, highlighting the membrane-binding role of the N-terminal tail. Our results show that the Y14 phosphorylation induces significant conformational changes to the N-terminal tail structure with enhanced inter-protomer hydrogen bonding resulting in an altered conformational state. The results provide mechanistic insights into how phosphorylation may act as a molecular switch that regulates Cav-1's structural behavior, membrane affinity, and caveolae biogenesis. - Source: PubMed
Publication date: 2026/05/06
Karki UkeshShabani SadeqDahal PrabinPadilla CathyHutcheson JoshuaChapagain Prem - Systemic sclerosis (SSc) is a severe autoimmune disease characterised by progressive fibrosis driven by fibroblast activation. Primary cilia, key hubs for profibrotic signalling, are markedly shortened in SSc fibroblasts, but the mechanisms underlying this phenotype remain unclear. This study aimed to define the signalling pathways responsible for primary cilia shortening and fibroblast activation in SSc. - Source: PubMed
Publication date: 2026/05/07
Wells RebeccaCaballero-Ruiz BegoñaMulipa PanjiTimmis Alex JTeves Maria EVarga JohnDel Galdo FrancescoRoss Rebecca LRiobo-Del Galdo Natalia A - The patch-clamp technique offers unparalleled insight into the electrical and biophysical behavior of excitable cells. However, it is a slow and low-throughput method that typically requires cells to be measured one by one. Human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CM) are regularly subjected to this technique to unravel the molecular mechanisms of cardiac diseases. Their use in direct patient treatment and successful drug development has been limited due to the lack of applicable high-throughput patch-clamp methods suited to successful hiPSC-CM measurement. Here we present a protocol employing a patch-clamp robot that addresses these limitations by using planar patch-clamp technology. We outline how to collect and handle hiPSC-CM for these experiments, along with optimized patch-clamp protocols for direct functional measurement of major cardiac ion channels including K2.1, Na1.5, Ca1.2, K11.1 and K3.1/3.4. We further explain how the liquid-handling properties of this setup allow multiple patch-clamp protocols to be combined in sequence while the cell remains in whole-cell configuration. This allows for over a hundred-fold increase in functional data acquisition. These procedures can be carried out within 1 d by both skilled and non-electrophysiologists; however, some experience in cell culture and handling is required. Overall, this protocol enhances fast and reliable functional characterization of hiPSCl-CM and may increase their applicability for rapid and safe drug development. - Source: PubMed
Publication date: 2026/05/07
Seibertz FitzwilliamSobitov IzzatuloGerloff Marcus LLiutkute AisteAlekseev AlexeyMager ThomasSchmidt ConstanzeFakuade Funsho EVoigt Niels