The nuclear pore complex (NPC) is the only gateway that connects the nucleus with the cytoplasm in eukaryotic cells. Its nucleoplasmic face is decorated by the nuclear basket, a filamentous structure with important roles in mRNA export and chromatin organization. In contrast to major parts of the nuclear pore scaffold, the architecture and organization of the nuclear basket remain poorly defined. In this study, we investigate the interaction network required for formation of the nuclear basket in vivo using budding yeast. We demonstrate that the filamentous Mlp1 protein relies on coiled-coil segments outside its previously characterized NPC-binding region to stably interact with the NPC. Furthermore, our results reveal that Mlp1's paralogue, Mlp2, plays a central role in nuclear basket architecture. Specifically, Mlp2 associates with the NPC independently of Mlp1 and together with Mlp1 is essential for the efficient recruitment of Pml39 and additional Mlp1 subunits. Our findings allow us to propose a refined model of nuclear pore basket architecture and organization.