Target intelligence / Profile preview

Ciliary rootlet coiled-coil protein (Rootletin) (CROCC)

Target
CROCC
Molecular classification
Structural molecule (cytoskeletal-associated protein), Coiled-coil protein, Other (not enzyme, receptor, or channel)
01

Overview

Ciliary rootlet coiled-coil protein (Rootletin), encoded by the CROCC gene, is a structural protein integral to the ciliary rootlet—a cytoskeletal-like structure originating from the basal body at the proximal end of a cilium and extending toward the nucleus. Rootletin is essential for maintaining centrosome cohesion before mitosis and for positioning the cilium basal body, thus facilitating ciliogenesis. Structurally, rootletin consists of a globular head domain and a tail domain made up of extended coiled-coil structures, enabling it to form homodimers and higher-order polymers that provide mechanical support in ciliated cells. It binds kinesin light chain 3 and physically interacts with C-Nap1 at centrioles; it is also phosphorylated by Nek2 kinase. Expression is selective to ciliated cells, including in the retina and respiratory epithelium. Mutations or deficiencies in Rootletin may be implicated in retinal diseases and genetic ciliopathies, such as Alstrom syndrome, although it is not currently considered a direct therapeutic drug target.

Other names
RootletinCROCCKIAA0445ROLTCROCC1Tax1-binding protein 2TAX1BP2Ciliary rootlet coiled-coil proteinCiliary rootlet protein
02

Mechanism of action

null

03

Biological functions

Formation and maintenance of ciliary rootletsCentrosome cohesion before mitosisKinesin bindingPositive regulation of cilium assemblyStructural maintenance of basal body position for ciliogenesisPositive regulation of protein localization to cilium
04

Disease associations

Retinal diseaseAlstrom syndromeOther ciliopathies

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