Target intelligence / Profile preview

CBY1-interacting BAR domain-containing protein 1 (CIBAR1)

Target
CIBAR1
Molecular classification
Other (BAR domain–containing protein, primarily considered a structural/membrane-associated adaptor protein)
01

Overview

CBY1-interacting BAR domain-containing protein 1 (CIBAR1) is a membrane-associated protein encoded by the FAM92A gene, notable for its BAR (Bin/Amphiphysin/Rvs) domain that enables binding to negatively charged phospholipids and induction of membrane curvature. CIBAR1 plays crucial roles in maintaining mitochondrial structure, organizing cristae, and is essential for ciliogenesis—localized to centrioles and the base of cilia, particularly relevant in sperm flagellar compartmentalization and proper annulus positioning, which is crucial for sperm motility. Mutations in CIBAR1 are associated with disorders such as postaxial polydactyly and certain ciliopathies. While classified structurally as a BAR domain–containing protein (not a classic receptor, enzyme, or transporter), its physiological significance is pronounced in mitochondrial morphology and ciliary function, particularly in reproductive and developmental processes. CIBAR1 is not currently considered a direct therapeutic target (such as a receptor or enzyme); it is a structural protein primarily involved in cell organization and development. There are no known drugs, small molecules, or established clinical biomarkers associated with this protein. No notable safety concerns or therapeutic challenges are currently documented for CIBAR1 inhibition or modulation in humans. CIBAR1 is a BAR domain-containing adaptor/scaffold protein essential for mitochondrial and ciliary structure, involved in male fertility, limb development, and congenital disorders linked to ciliogenesis defects, but is not a classical drug target.

Other names
FAM92AFAM92A1FLJ38979BARMR1PAPA9family with sequence similarity 92 member Aprotein FAM92Aprotein FAM92A1
02

Biological functions

Regulation of mitochondrial ultrastructure and cristae organizationPhospholipid binding, especially negatively charged phospholipidsMembrane curvature and tubulationCiliogenesis and cilium assemblySperm flagellum compartmentalization and integrity (annulus positioning)Limb morphogenesis
03

Disease associations

Genetic variants associated with polydactyly (postaxial, type A1 and A9)Reported mutations in ciliopathies (including Joubert syndrome, polydactyly)

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