Ask about this productRelated genes to: C21orf59 antibody
- Gene:
- CFAP298 NIH gene
- Name:
- cilia and flagella associated protein 298
- Previous symbol:
- C21orf48, C21orf59
- Synonyms:
- FLJ20467, FBB18, CILD26, Kur
- Chromosome:
- 21q22.11
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-28
- Date modifiied:
- 2018-02-02
Related products to: C21orf59 antibody
Related articles to: C21orf59 antibody
- Cfap298 is a highly conserved gene required for ciliary motility and dynein arm assembly, with known roles in left-right (LR) patterning in zebrafish and links to human ciliopathies. Here, we describe a Cfap298 mutant allele, Cfap298ΔΔS, which selectively disrupts LR axis establishment in mice. Mutant embryos display organ laterality defects and abnormal Nodal, Pitx2 and Lefty1 expression, consistent with an early disruption in LR symmetry breaking. LR asymmetry is established by leftward fluid flow in the node, generated by planar-polarized cilia. Although cfap298 mutations are reported to affect planar polarity, we did not observe changes in cilia position, length or CELSR1 localization within the node, suggesting that Cfap298ΔΔS functions at the level of cilia motility. Accordingly, cilia lining the trachea of Cfap298ΔΔS mutants fail to beat or beat incorrectly. Expression of the Cfap298ΔΔS variant in zebrafish partially rescues body curvature defects but fails to rescue LR defects of cfap298 (kurly) loss-of-function mutants. These results confirm a conserved role for Cfap298 in mammalian LR patterning and identify a previously unreported region of CFAP298 with a conserved and essential role in cilia motility. - Source: PubMed
Publication date: 2025/10/31
Cortez MarvinYoung Cullen BLittle Katherine AGrimes Daniel TDevenport DanelleBurdine Rebecca D - is a highly conserved gene required for ciliary motility and dynein arm assembly. It plays a known role in Left-Right (LR) patterning in zebrafish and is linked to human ciliopathies. Here we describe a new mutant allele, , which selectively interferes with LR axis establishment in mice. Mutant embryos display a range of laterality defects including , , and , as indicated by abnormal heart, lung, and stomach positioning. At embryonic day 8.5, mutant embryos display abnormal , , and expression patterns in the lateral plate mesoderm and midline, consistent with an early disruption in LR symmetry breaking. In mice, LR asymmetry is established by leftward fluid flow in the node, generated by planar-polarized cilia. Although mutations are reported to affect cell polarity, we did not observe changes in cilia position, length, or planar cell polarity protein localization within the node, suggesting that functions at the level of cilia motility. Consistently, motile cilia lining the trachea of mutants fail to beat. Expression of the variant in zebrafish fails to rescue the LR defects of ( loss-of-function mutants. These results confirm that functions in LR axis formation in mammals and uncover a novel region of CFAP298 protein with a conserved and essential role in cilia motility. - Source: PubMed
Publication date: 2025/05/17
Cortez MarvinYoung Cullen BLittle Katherine AGrimes Daniel TDevenport DanelleBurdine Rebecca D
- Source: PubMed
- Motile cilia are organelles found on many eukaryotic cells that play critical roles in development and fertility. Human CFAP298 has been implicated in the transport/assembly of ciliary dyneins, and defects in this protein cause primary ciliary dyskinesia. However, neither the exact function nor the structure of CFAP298 have been elucidated. Here, we took advantage of , a ciliated alga, to study the structure and function of FBB18, an ortholog of CFAP298. Multiple ciliary dyneins were greatly reduced in cilia of mutants. In addition, we found that both the stability of ciliary dynein heavy chains (HCs) and the association between HCs and intermediate/light chains (IC/LCs) are greatly reduced in cytoplasm, strongly suggesting that FBB18 functions in the cytoplasmic assembly (the so-called "preassembly") of dynein complexes from HC/IC/LCs. Furthermore, X-ray crystallography revealed that FBB18 forms a bilobed structure with globular domains at both ends of the molecule, connected by an α-helical bundle. Unexpectedly, one globular domain shows high similarity to ubiquitin, a small protein critical for the modification of a variety of protein complexes, and this ubiquitin-like domain is indispensable for the molecular function of FBB18. Our results demonstrate that FBB18, a specialized member of the ubiquitin-like protein family, plays a critical role in dynein preassembly, most likely by mediating diverse interactions between dynein HCs, molecular chaperone(s), and other preassembly factor(s) using the ubiquitin-like domain as well as other regions, and by facilitating the proper folding of dynein HCs. - Source: PubMed
Publication date: 2025/03/19
Yamamoto RyosukeSahashi YuiShimo-Kon RiekoSakato-Antoku MihoSuzuki MiyukaLuo LeoTanaka HideakiIshikawa TakashiYagi ToshikiKing Stephen MKurisu GenjiKon Takahide - Canine osteosarcoma (OSA) is an aggressive bone neoplasia with high metastatic potential. Metastasis is the main cause of death associated with OSA, and there is no current treatment available for metastatic disease. Proteomic analyses, including matrix-assisted laser desorption/ionisation-time of flight mass spectrometry (MALDI TOF/TOF MS), are widely used to select molecular targets and identify proteins that may play a key role in primary tumours and at various steps of the metastatic cascade. The main aim of this study was to identify proteins differently expressed in canine OSA cell lines with different malignancy phenotypes (OSCA-8 and OSCA-32) compared to canine osteoblasts (CnOb). The intermediate aim of the study was to compare canine OSA cell migration capacity and assess its correlation with the malignancy phenotypes of each cell line. Using MALDI-TOF/TOF MS analyses, we identified eight proteins that were significantly differentially expressed ( ≤ 0.05) in canine OSA cell lines compared to CnOb: cilia- and flagella-associated protein 298 (CFAP298), general transcription factor II-I (GTF2I), mirror-image polydactyly gene 1 protein (MIPOL1), alpha-2 macroglobulin (A2M), phosphoglycerate mutase 1 (PGAM1), ubiquitin (UB2L6), ectodysplasin-A receptor-associated adapter protein (EDARADD), and leucine-rich-repeat-containing protein 72 (LRRC72). Using the Simple Western technique, we confirmed high A2M expression in CnOb compared to OSCA-8 and OSCA-32 cell lines (with intermediate and low A2M expression, respectively). Then, we confirmed the role of A2M in cancer cell migration by demonstrating significantly inhibited OSA cell migration by treatment with A2M (both at 10 and 30 mM concentrations after 12 and 24 h) in a wound-healing assay. This study may be the first report indicating A2M's role in OSA cell metastasis; however, further in vitro and in vivo studies are needed to confirm its possible role as an anti-metastatic agent in this malignancy. - Source: PubMed
Publication date: 2024/04/03
Wilk Sylwia SMichalak KatarzynaOwczarek Ewelina PWiniarczyk StanisławZabielska-Koczywąs Katarzyna A