ArticleMolecular and cellular biology2016
BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis.
Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 51 citations in OpenAlex.
- FAM92A Underlies Nonsyndromic Postaxial Polydactyly in Humans and an Abnormal Limb and Digit Skeletal Phenotype in Mice.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019Trial
- The planar cell polarity protein Vangl2 interacts with the PDZ-domains of Scribble but not with a unique PDZ-like domain in Inturned.FEBS letters · 2026Article
- Basal body docking failure triggers centriole clustering and elimination in mammalian spermatogenesis.EMBO reports · 2026Article
- GRAF1-dependent endocytotic processes and the Golgi apparatus contribute to previously unrecognized intermediate stages of early ciliogenesis.Nature communications · 2026Article
- Loss of cilia drives centriole clustering and elimination during mammalian spermatogenesis.bioRxiv : the preprint server for biology · 2025Article
- Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.Science advances · 2025Article
- The human ciliopathy protein RSG1 links the CPLANE complex to transition zone architecture.Nature communications · 2025Article
- ciBAR1 loss in mice causes laterality defects, pancreatic degeneration, and altered glucose tolerance.Life science alliance · 2025Article
- Circular RNAs: novel noncoding players in male infertility.Hereditas · 2024Review
- Membrane remodeling by FAM92A1 during brain development regulates neuronal morphology, synaptic function, and cognition.Nature communications · 2024Article
- The ARPKD Protein DZIP1L Regulates Ciliary Protein Entry by Modulating the Architecture and Function of Ciliary Transition Fibers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The relationship between intraflagellar transport and upstream protein trafficking pathways and macrocyclic lactone resistance in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2024Article
- The Cby3/ciBAR1 complex positions the annulus along the sperm flagellum during spermiogenesis.The Journal of cell biology · 2024Article
- Cep131-Cep162 and Cby-Fam92 complexes cooperatively maintain Cep290 at the basal body and contribute to ciliogenesis initiation.PLoS biology · 2024Article
- Global Proteomics Analysis of Lysophosphatidic Acid Signaling in PC-3 Human Prostate Cancer Cells: Role of CCN1.International journal of molecular sciences · 2024Article
- Ciliogenesis membrane dynamics and organization.Seminars in cell & developmental biology · 2023Review
- Appearing and disappearing acts of cilia.Journal of biosciences · 2023Review
- Composition, organization and mechanisms of the transition zone, a gate for the cilium.EMBO reports · 2022Review
- Mutations in SCNM1 cause orofaciodigital syndrome due to minor intron splicing defects affecting primary cilia.American journal of human genetics · 2022Article
- Structural validation and assessment of AlphaFold2 predictions for centrosomal and centriolar proteins and their complexes.Communications biology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Chibby1 (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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.