CEP97 antibody
- Known as:
- CEP97 (anti-)
- Catalog number:
- orb100629
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- CEP97 antibody
Related genes to: CEP97 antibody
- Gene:
- CEP97 NIH gene
- Name:
- centrosomal protein 97
- Previous symbol:
- LRRIQ2
- Synonyms:
- FLJ23047
- Chromosome:
- 3q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-09-01
- Date modifiied:
- 2016-03-30
Related products to: CEP97 antibody
Related articles to: CEP97 antibody
- The trafficking, docking, and fusion of membrane vesicles at the mother centriole (MC) are important for primary cilium construction. Here, we determined the three-dimensional (3D) membrane ultrastructures, and associated proteins, involved in this primary cilium assembly mechanism upstream of axoneme growth. Our work suggests that the enlargement of small vesicles docked to the MC is a key trigger for ciliogenesis progression, a process requiring the MC distal appendage protein CEP164. These vesicles appear to fuse to form tubular C-shaped intermediates and an unprecedented toroidal membrane intermediate. The formation of these previously uncharacterized tubular membrane ciliogenesis intermediates is orchestrated by the membrane trafficking regulators EHD1 and RAB8, and is associated with the IFT-B complex protein IFT88. Remarkably, we show that EHD1, through its membrane tubulation function, regulates ciliogenesis progression by directly promoting CP110/CEP97 removal from the MC cap. The establishment of these tubular membrane structures is also associated with the recruitment of the ciliary gate transition zone proteins. Together, these findings redefine the architectural framework of early ciliogenesis and underscore the utility of isotropic ultrastructural imaging combined with quantitative 3D analysis for elucidating mechanisms of membrane trafficking and organelle biogenesis. - Source: PubMed
Publication date: 2026/06/13
Lu QuanlongZhao HuijieKhan ZiamHarned AdamKamiya ErinaMagidson ValentinSenthilkumar AbhiKilnagar AvaneeshDoan Phuong Thi BichPerera SumethNarayan KedarWestlake Christopher J - Centrioles maintain a characteristic length throughout the cell cycle, which is essential for the accurate functioning of centrosomes and ciliogenesis. The CP110-Cep97 complex acts as a cap on the distal end of the centriole, restricting microtubule extension. However, whether CP110-Cep97 alone or in conjunction with additional players regulates this process remains unclear. In this study, we identify the kinase Nek1 (NIMA-related kinase 1) as a key factor that works with the CP110-Cep97 complex to control centriole length. Nek1 localizes alongside CP110 and Cep97 at the distal end of the centriole and interacts with Cep97 and Cep78. Loss of Nek1 induces pronounced centriolar microtubule hyperelongation without displacement of the CP110-Cep97 complex, indicating that Nek1 restricts centriole extension through a distinct mechanism. Co-depletion of Nek1 and CP110, but not Cep78, further enhances the hyperelongation phenotype, demonstrating that Nek1 and CP110 pathways act in parallel to maintain centriole length in cycling cells. Notably, Nek1 is removed from the basal body during ciliogenesis in a Cep78-dependent manner, thereby linking Cep78 to the spatial regulation of Nek1 activity. Together, these findings establish Nek1 as an important safeguard that works with the CP110-Cep97 complex to ensure the structural integrity of centrioles. - Source: PubMed
Publication date: 2026/06/09
Streubel J M SKarasu O RMunoz I MNeuner ANumanoglu E NMacartney T JSchiebel ERouse JPereira G - Architecture is critical for organelle function. The lengths of centrioles, key components of centrosomes, are tightly regulated. We adapted centrosome purification approaches to measure centrosomal protein phosphorylation. Centrosome-specific phosphoproteomics with and without cyclin-dependent kinase 1 (CDK1) activity revealed that CDK1 phosphorylates many centriolar proteins involved in centriole length control, including Centrobin. CDK1 regulated centriole length synergistically with CEP97-CCP110, a local centriolar complex. CEP97 restricted Centrobin localization to centrioles, whereas CDK1-dependent phosphorylation suppressed Centrobin's ability to promote centriole elongation. Thus, CDK1 and CEP97-CCP110 both restrict centriole elongation by inhibiting the function of Centrobin, a centriole elongation factor, but via different mechanisms. Overelongated centrioles failed to support ciliogenesis in human cells and in mouse embryos. Removing CEP97 during mouse development caused centriole overelongation, impaired ciliogenesis and attenuated Hedgehog (HH) signaling, disrupting mouse heart development. We conclude that CEP97-CCP110 and CDK1 cooperatively restrict Centrobin function to control centriole length, critical for mammalian development. - Source: PubMed
Publication date: 2026/05/15
Liu YueWang ZhengmaoSinha TanviLi Kathy HChalkley Robert JHerranz-Pérez VicenteXie ChangYoder Bradley KBurlingame Alma LBlack Brian LReiter Jeremy F - A significant challenge in studying the biology of the Drosophila centriole is its small size. Advanced super-resolution techniques have provided valuable insights but require specialized equipment and can be difficult to implement in tissues. Expansion microscopy (ExM) offers an accessible alternative, yet its application in Drosophila centriole research has been sparse. We provide an ExM protocol for cultured S2 cells and fly tissues that reveals new insights into procentriole biology. In S2 cells we document overduplication in the form of the classic 'rosettes', while in spermatids we uncover an unexpected movement of the procentriole-like structure (PCL). ExM has also refined existing molecular models. In S2 cells we document the distal tip protein Cep97 as a ring, which clarifies its role in capping the growing centriole. In spermatids, we spatially segregate the inner nuclear membrane protein Spag4 and the cytoplasmic protein Yuri, leading to the new hypothesis that they play independent roles at the centriole-nucleus contact site. Finally, we show that our ExM protocol is a hypothesis generator and discovery tool applicable beyond Drosophila centrioles by imaging synaptonemal complexes in the Plodia interpunctella moth. - Source: PubMed
Publication date: 2026/01/19
Burns Emma EAmoiroglou AnastasiaFagerstrom Carey JRyniawec John MLee LingSzeRunyan Rose KRosin Leah FRogers Gregory CRusan Nasser M - Dysfunction at the centrosome-cilium interface underlies a broad range of ciliopathies. Here, we identify biallelic variants in , encoding a centrosomal protein, in eight unrelated individuals presenting with neurodevelopmental, ocular, and variable additional multisystem features. Proband-derived fibroblasts and CEP76-depleted RPE1 cells display ciliary deficits, including impaired cilium formation and length, disrupted transition zone architecture, and impaired IFT88-mediated anterograde intraflagellar transport. Zebrafish mutants recapitulate key clinical phenotypes, and in vitro complementation assays confirm pathogenicity for all tested human disease-associated variants. Proteomics analysis identifies CEP76 interactors, including known partners CCP110 and CEP97, and highlights clinically and functionally relevant candidates, including ALMS1 and LUZP1. Together, these findings expand the role of CEP76 beyond centriole duplication to include ciliary assembly and trafficking, establishing it as a ciliopathy gene. This work provides mechanistic insights into -related disease and broadens our understanding of centrosome-cilium biology. - Source: PubMed
Publication date: 2025/10/17
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