Ask about this productRelated genes to: IFT88 Blocking Peptide
- Gene:
- IFT88 NIH gene
- Name:
- intraflagellar transport 88
- Previous symbol:
- TTC10
- Synonyms:
- hTg737, Tg737, D13S1056E, MGC26259
- Chromosome:
- 13q12.11
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-16
- Date modifiied:
- 2016-10-05
Related products to: IFT88 Blocking Peptide
Related articles to: IFT88 Blocking Peptide
- Microbial rhodopsin-based optogenetics has been widely applied to diverse mammalian and plant cell types for controlling membrane potential mediated responses. Microbial rhodopsin fusions like RhoPDE, and RhoGC (enzyme rhodopsins) have also been used for spatiotemporal modulation of cyclic nucleotide signaling non-invasively across the biological systems. Complex microbial rhodopsins like Chlamyopsin5 and Chlamyopsin6 are modular in nature and rhodopsin is coupled with the two-component signaling module (histidine kinase and response regulator), and cyclase domain in a tandem. However, functional characterization and cellular trafficking of these optogenetically active proteins to the desired subcellular organelle is still a major concern in optogenetics field. Current study is focused on the trafficking of two of the complex microbial modular rhodopsins (Chalmyopsin5 and Chlamyopsin6) in a green alga, Chlamydomonas reinhardtii. Immunolocalization of Chlamyopsin5 and Chlamyopsin6 in wild strain suggests their differential subcellular localization; Chlamyopsin5 is mainly in eyespot and Chlamyopsin6 is localized both in flagella and eyespot. Extensive immunocytochemistry of Chlamyopsin5 and Chlamyopsin6 was performed in different intraflagellar transport (IFT) components-defective strains of Chlamydomonas to dissect their trafficking and localization. Our results indicated the trafficking of Chlamyopsin5 to the eyespot is independent of IFT machinery while IFT machinery drives localization of Chlamyopsin6 to the flagella. Further, we demonstrate that IFT88 and IFT52 stabilizes turnover of Chlamyopsin6 and IFT20 interacts with Chlamyopsin6 in Chlamydomonas. Collectively, our study enabled us to understand the targeting of large Chlamyopsins to the subcellular compartment (eyespot and flagella). This study pave way to expand optogenetic applications of these complex microbial-type modular rhodopsins for opto-modulation of two-components mediated physiological processes. - Source: PubMed
Publication date: 2026/05/27
Sushmita KumariSharma SunitaSingh RajaniKateriya Suneel - Intervertebral disc (IVD) degeneration (IDD) involves nucleus pulposus (NP) cell death, but its mechanisms are unclear. PANoptosis is a novel cell death pattern whose role in IDD remains elusive. This study investigates whether PANoptosis contributes to mechanical overloading-induced NP cell death and explores its underlying mechanisms. We evaluated PANoptosis in NP cells from human degenerated IVD tissues, aged mice, lumbar spine instability model, and an mechanical compression system. Results indicated that PANoptosis-related proteins were upregulated in NP cells from degenerated IVDs, as well as in those subjected to mechanical overloading both and . To confirm its functional role, we inhibited PANoptosis by interfering PANoptosis sensor Z-DNA-binding protein 1 (ZBP1). Results showed that ZBP1 inhibition partially reversed this upregulation, reduced NP cell death, and alleviated IDD. Mechanistically, we found Kindlin-2 loss promoted PANoptosis in NP cells by suppressing forkhead box P1 (FOXP1) SUMOylation and increasing ZBP1 promoter activity. Furthermore, mechanical overloading downregulated Kindlin-2 by impairing ciliary intraflagellar transport 88 (IFT88), thereby exacerbating PANoptosis and IDD. We show that ciliary IFT88 influences Kindlin-2, which protects NP cells from mechanical overloading-induced PANoptosis by enhancing FOXP1 SUMOylation. This pathway may offer a new therapeutic target for IDD. - Source: PubMed
Publication date: 2026/04/16
Li KangluChen MingjueChen ChaoYu YihanLiu ShengShao ZengwuCai XianyiXiao GuozhiChen Sheng - Spinal disorders such as intervertebral disc degeneration (IVDD) and scoliosis cause significant disability and socioeconomic burden. Current treatments are palliative, which reflects a limited understanding of the cellular mechanisms underlying the disease. Primary cilia are critical mechanosensory organelles. However, their contribution to intervertebral disc pathology and spinal deformities remains unclear. - Source: PubMed
Publication date: 2026/05/16
Li XinhuaGuo KaiYang YangYang Shu-TingMao KeyaQin LingLi LijunHuang YufengHang DonghuaYang Shuying - Neutralizing sclerostin antibodies (Scl-Ab) mitigate bone loss and promote bone formation to address fracture risk in postmenopausal osteoporosis. Clinically, this treatment is administered monthly for women at high risk of fragility fractures, who are often years into menopause. Preclinical studies have demonstrated that dampening of bone formation occurs with continuous dosing at supraphysiological doses. Osteoporotic bone loss occurs rapidly during early menopause, followed by longer-term changes in bone mineralization and osteocyte activity. Whether earlier administration of lower-exposure Scl-Ab can mitigate bone loss and osteocyte-mediated mineralization is unknown. The objective of this study was to evaluate the effects of early intermittent low-dose Scl-Ab on: (1) osteoclastogenesis and bone resorption, (2) perilacunar remodelling, (3) secondary mineralization, and (4) osteocyte mechanosensitivity. Female retired breeder Wistar rats underwent bilateral ovariectomy and received monthly low-dose Scl-Ab injections (2 mg/kg/month) from 3 to 14 weeks post-OVX, while a control group remained untreated. Early intermittent low-dose Scl-Ab treatment increased bone formation and reduced osteoclastogenesis and catabolic gene expression ((Sost, Ctsk, Mmp9) compared to untreated rats. Treatment also decreased the percentage of empty lacunae and the number of MMP14+ osteocytes, accompanied by lower perilacunar mineral density and smaller lacunar size, indicating improved osteocyte survival and reduced perilacunar remodelling. Conversely, expression of osteocyte-mediated mineralization genes (DMP1, PHEX, OPN, ALP) and mechanotransduction-related genes (Vcl, integrins α5, αV, β1, CX43, Axin2, IFT88, Adcy6, Pkd1, Cav1) were reduced. Together, these findings suggest that early intermittent low-dose Scl-Ab therapy promotes surface bone formation while attenuating osteocyte-mediated mineralization after initial bone loss. - Source: PubMed
Publication date: 2026/04/07
Naqvi Syeda MasoomaAli WahaajAllison HollieO'Sullivan Laura MHoldsworth GillPanadero-Perez Juan AlbertoSchiavi-Tritz JessicaMcNamara Laoise M - Tubulin post-translational modifications confer diverse functions to microtubules, with polyglutamylation representing a dynamic modification governed by coordinated glutamylation and deglutamylation. AGBL5 functions as a deglutamylase that removes glutamate residues at branch points within polyglutamate chains. While pathogenic variants in human are associated with retinitis pigmentosa, the underlying mechanism remains poorly defined. In the present study, an knockout mouse model was established and exhibited pronounced tubulin hyperglutamylation in photoreceptors, followed by progressive retinal degeneration. Transcriptomic profiling identified widespread disruption of ciliary function in knockout mice. Ultrastructural analysis by transmission electron microscopy revealed an impaired inner scaffold within the connecting cilium. Consistent with this defect, key phototransduction proteins were mislocalized or down-regulated in both mutant rod and cone photoreceptors, accompanied by severe disorganization of outer segment disk membranes. Immunofluorescence further demonstrated impaired recruitment of IFT88, kinesin-II, and dynein-2 to the connecting cilium, suggesting defective intraflagellar transport. Collectively, these findings indicate that AGBL5-dependent tubulin glutamylation homeostasis is essential for photoreceptor survival through preservation of connecting cilium architecture and normal protein trafficking mediated by intraflagellar transport. - Source: PubMed
Publication date: 2026/02/10
Wang Hao-LinWang TingZhen Fang-YuanLin Yong-QiongTong Ying-JieWu Jia-HuiGuo Jia-XinWang Jia-JiaDong Shu-QianJanke CarstenMagiera Maria MZhang Hou-BinZou Tong-Dan