Cby1 promotes Ahi1 recruitment to a ring-shaped domain at the centriole–cilium interface and facilitates proper cilium formation and function

Lee, Yin Loon; Sante, Joshua M.; Comerci, Colin J.; Cyge, Benjamin; Menezes, Luís F.; Li, Feng Qian; Germino, Gregory G.; Moerner, W. E.; Takemaru, Ken Ichi; Stearns, Tim

doi:10.1091/mbc.e14-02-0735

Cited by 57 publications

(71 citation statements)

References 73 publications

(113 reference statements)

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“…3C). FAM92A showed extensive colocalization with Cby1 at mother centrioles while displaying a partial overlap with CEP164, which localizes to the distal appendages of mother centrioles (5,6,14,15,20). Furthermore, the results from costaining with different centrosome/centriole markers, including G-tub (centrosomes), CEP135 (proximal ends of centrioles), and centrobin (daughter centrioles), support the notion that FAM92A localizes to the distal end of mother centrioles.…”

Section: Identification Of Fam92a As a Cby1-interacting Proteinsupporting

confidence: 61%

“…Chibby1 (Cby1) is a conserved 15-kDa coiled-coil protein that predominantly localizes to mother centrioles/basal bodies and plays a pivotal role in the formation and function of cilia (6,(12)(13)(14)(15)(16)(17)(18)(19). Cby1 knockout (Cby1-KO) mice display several hallmarks of ciliary defects, including chronic upper airway infection (12), subfertility, and polycystic kidneys (15) as well as polydactyly and hydrocephalus at low frequencies.…”

mentioning

confidence: 99%

“…Cby1 knockout (Cby1-KO) mice display several hallmarks of ciliary defects, including chronic upper airway infection (12), subfertility, and polycystic kidneys (15) as well as polydactyly and hydrocephalus at low frequencies. In Drosophila melanogaster, Cby1 is expressed in sensory neurons and male germ cells, the only ciliated cell types in this organism, and is required for the proper formation of neuronal cilia and sperm flagella, respectively (16).…”

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confidence: 99%

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BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Chen

Fisher

et al. 2016

Molecular and Cellular Biology

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dChibby1 (Cby1) is a small, conserved coiled-coil protein that localizes to centrioles/basal bodies and plays a crucial role in the formation and function of cilia. During early stages of ciliogenesis, Cby1 is required for the efficient recruitment of small vesicles at the distal end of centrioles to facilitate basal body docking to the plasma membrane. Here, we identified family with sequence similarity 92, member A (FAM92A) and FAM92B, which harbor predicted lipid-binding BAR domains, as novel Cby1-interacting partners using tandem affinity purification and mass spectrometry. We found that in cultured cell lines, FAM92A colocalizes with Cby1 at the centrioles/basal bodies of primary cilia, while FAM92B is undetectable. In airway multiciliated cells, both FAM92A and -92B colocalize with Cby1 at the base of cilia. Notably, the centriolar localization of FAM92A and -92B depends largely on Cby1. Knockdown of FAM92A in RPE1 cells impairs ciliogenesis. Consistent with the membrane-remodeling properties of BAR domains, FAM92A and -92B in cooperation with Cby1 induce deformed membrane-like structures containing the small GTPase Rab8 in cultured cells. Our results therefore suggest that FAM92 proteins interact with Cby1 to promote ciliogenesis via regulation of membrane-remodeling processes.

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Section: Identification Of Fam92a As a Cby1-interacting Proteinsupporting

confidence: 61%

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confidence: 99%

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confidence: 99%

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BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Chen

Fisher

et al. 2016

Molecular and Cellular Biology

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“…35,36 Cby1 localizes to the base of cilia and plays a crucial role in ciliogenesis. [18][19][20][21][22] More recently, we demonstrated that, during differentiation of airway ciliated cells, Cby1 localizes to nascent centrioles and interacts with Rabin8, a guanine nucleotide exchange factor (GEF) for the small GTPase Rab8 to promote Rab8 recruitment for efficient assembly of membranous structures, called ciliary vesicles, at the distal end of centrioles. 18 Intriguingly, Rab8 has been shown to regulate cell shape, and expression of dominant-negative Rab8 mutants or depletion of Rab8 by small interfering (si) RNAs promotes an epithelial cell-like morphology including tight cell-cell contacts and actin stress fiber formation.…”

Section: Discussionmentioning

confidence: 99%

“…Cby1 also plays a crucial role during ciliogenesis, likely independent of b-catenin signaling. [18][19][20][21][22] Using human colon adenocarcinoma SW480 cells in which APC is mutated, we reported that stable expression of wildtype Cby1, but not a 14-3-3-binding-defective mutant (Cby1S20A), results in cytoplasmic translocation of b-catenin, concomitant with a reduction in b-catenin signaling and cell growth. 23 These results suggest a role for Cby1 as a tumor suppressor in colon cancer.…”

Section: Introductionmentioning

confidence: 99%

Chibby1 knockdown promotes mesenchymal-to-epithelial transition-like changes

Fischer

Wong

et al. 2017

Cell Cycle

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Chibby1 (Cby1) was originally isolated as a binding partner for b-catenin, a dual function protein in cell-cell adhesion and in canonical Wnt signaling. The canonical Wnt/b-catenin pathway is dysregulated in various diseases including cancer, most notably of the gastrointestinal origin. To investigate the role of Cby1 in colorectal tumorigenesis, we generated stable Cby1-knockdown (K D ) SW480 colon cancer cells. Unexpectedly, we found that Cby1 K D induces mesenchymal-to-epithelial transition (MET)-like changes in SW480 as well as in HEK293 cells. Cby1-K D cells displayed a cuboidal epithelial morphology with tight cellcell contacts. In Cby1-K D cells, the plasma membrane localization of E-cadherin and b-catenin was dramatically increased with formation of cortical actin rings, while the levels of the mesenchymal marker vimentin were decreased. Consistent with these changes, in wound healing assays, Cby1-K D cells exhibited epithelial cell-like properties as they migrated collectively as epithelial sheets. Furthermore, the anchorage-independent growth of Cby1-K D cells was reduced as determined by soft agar assays. These findings suggest that chronic Cby1 K D in colon cancer cells may counteract tumor progression by promoting the MET process.

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Clinical and molecular findings in a cohort of 152 Brazilian severe early onset inherited retinal dystrophy patients

Sallum

Motta

Arno

et al. 2020

American J of Med Genetics Pt C

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Leber congenital amaurosis (LCA) and early-onset retinal dystrophy (EORD) are severe inherited retinal dystrophy that can cause deep blindness childhood. They represent 5% of all retinal dystrophies in the world population and about 10% in Brazil. Clinical findings and molecular basis of syndromic and nonsyndromic LCA/EORD in a Brazilian sample (152 patients/137 families) were studied. In this population, 15 genes were found to be related to the phenotype, 38 new variants were detected and four new complex alleles were discovered. Among 123 variants found, the most common were CEP290: c.2991+1655A>G, CRB1: p.Cys948Tyr, and RPGRIP1: exon10-18 deletion. K E Y W O R D S causal genes, childhood blindness, early-onset retinal dystrophy (EORD), genotypephenotype, Leber congenital amaurosis (LCA), pathogenic variants 1 | INTRODUCTION Leber congenital amaurosis (LCA) is the most severe and earliest onset inherited retinal dystrophy. Affected individuals usually present, in the first year of life with severe visual impairment, nystagmus and occasionally a systemic manifestation (Francis, 2006). Phenotypic variability in fundus abnormality, refractive errors, photophobia or lightseeking behavior, nyctalopia, nystagmus, low visual acuity, and Franceschetti's oculo-digital sign, are also commonly observed in these patients (Chung & Traboulsi, 2009; den Hollander, Roepman, Koenekoop, & Cremers, 2008). Early-onset retinal dystrophy (EORD) can be considered as belonging to the same LCA spectrum but a milder form, where signs and symptoms appear after the first year of life up to 5-7 years-old (Weleber, Francis, Trzupek, & Beattie, 2004), but still a disease that severely compromises vision. Clinically, LCA and EORD are similar and may represent a continuum; the distinction between them is an extinguished or markedly diminished ERG response before the first year of life for individuals with

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Cby1 promotes Ahi1 recruitment to a ring-shaped domain at the centriole–cilium interface and facilitates proper cilium formation and function

Cited by 57 publications

References 73 publications

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Chibby1 knockdown promotes mesenchymal-to-epithelial transition-like changes

Clinical and molecular findings in a cohort of 152 Brazilian severe early onset inherited retinal dystrophy patients

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