Leucine-rich repeat-containing protein 45 (LRRC45)

Leucine-rich repeat-containing protein 45 (LRRC45) is a structural protein involved in maintaining centrosome cohesion and regulating ciliogenesis, but it is not a classical receptor, enzyme, transporter, or established therapeutic drug target. LRRC45 localizes at the proximal ends of centrioles in the centrosome, where it forms fiber-like structures linking duplicated centrosomes during interphase and promotes their function as a single microtubule-organizing center. Upon mitotic entry, LRRC45 is phosphorylated by the kinase Nek2A, leading to dissociation from the centrosome and enabling centrosome separation. LRRC45 also acts in ciliogenesis by being recruited to the mother centriole, where it is required for the recruitment of other ciliogenesis factors and for organizing centriolar satellites, thus facilitating cilia formation. Modulation of LRRC45 function can occur via alternative splicing and post-translational modifications. Diseases genetically associated with LRRC45 mutations include Bardet-Biedl syndrome and Nephronophthisis 18, both ciliopathies, but no direct drug interactions, therapeutic targeting, or biomarker roles are currently described for this protein.

Other names

LRRC45MGC20806leucine rich repeat containing 45LRC45_HUMAN