Centrioles are conserved microtubule-based organelles essential for key cellular processes such as cell division and ciliogenesis. Human centrioles exhibit a distinct cylindrical architecture composed of nine microtubule triplets arranged around a central axis and are polarized along the proximal-distal axis with defined substructural elements. Despite their importance, the detailed molecular organization of centrioles and the roles of many of their components remain incompletely understood. To address this, we combined Ultrastructure Expansion Microscopy (U-ExM) with a time-series reconstruction approach to generate a high-resolution map of the human centriole during its assembly. This strategy enabled the nanoscale spatial assignment of 24 centriolar proteins, revealing their longitudinal and radial positions across different stages of the cell cycle. The resulting map uncovered new structural insights and allowed us to link specific proteins to defined substructures of the centriole. Focusing on the A-C linker, a previously enigmatic structure that connects adjacent microtubule triplets of the proximal region, we identified several candidate proteins. Among them, we characterized two previously identified centriolar proteins, CCDC77 and WDR67, and discovered MIIP as an A-C linker component. These proteins localize to the proximal region of the centriole and occupy the space between neighboring microtubule triplets. Functional studies demonstrated that these components are crucial for centriole cohesion, as their depletion leads to microtubule disorganization and structural fragmentation. Moreover, we uncovered a novel role for A-C linker proteins in regulating centriole duplication via modulation of the torus structure. In summary, I uncovered the molecular composition of the A-C linker and its multifunctional roles in maintaining centriole integrity and in centriole duplication.