LRRC45 (leucine-rich repeat containing 45) is a multifunctional centrosomal protein with distinct roles in centrosome architecture and ciliogenesis. Structurally, LRRC45 localizes at the proximal ends of centrioles, where it forms fiber-like proteinaceous linker structures essential for centrosome cohesion 1. During interphase, LRRC45 interacts with C-Nap1 and rootletin to maintain centrosome integrity; depletion causes centrosome splitting 1. During mitosis, Nek2A phosphorylation of LRRC45 at S661 triggers its dissociation and centrosome separation 1. Beyond centrosome cohesion, LRRC45 contributes to ciliogenesis through distal appendage localization 2. Recruited by core appendage proteins Cep83 and SCLT1, LRRC45 organizes centriolar satellites, establishes the transition zone, and promotes Rab8-positive vesicle docking—functions distinct from CP110 removal 23. Clinically, biallelic LRRC45 variants cause severe neurological ciliopathy; loss-of-function mutations reduce primary cilia frequency and impair ciliogenesis 4. Additionally, LRRC45 is upregulated in lung and bladder cancers, promoting proliferation and metastasis through c-MYC, Slug, MMP2/9 upregulation (lung cancer) and NRF2 stabilization via KEAP1 competition (bladder cancer), correlating with poor prognosis 56.