The study reveals how the kinase Mps1 is recruited to the kinetochore to enable mitotic checkpoint signaling. Upon formation of bi-oriented kinetochore-microtubule attachments, the Dam1 complex displaces Mps1 from its binding site on the Ndc80 complex, promoting anaphase onset. The N-terminal segment of Mps1 binds the neck region of Ndc80:Nuf2, the main microtubule receptor of kinetochores. Mutational disruption of this interface prevents Mps1 localization, eliminates SAC signaling, and impairs growth. The same interface of Ndc80:Nuf2 binds the Dam1 complex. The error correction kinase Ipl1 phosphorylates the Dam1 C terminus, preventing Dam1 from displacing Mps1 during error correction. The binding of the Dam1 complex to Ndc80:Nuf2 may release Mps1 from the kinetochore to promote anaphase onset. The study identifies the binding interface between Mps1 and Ndc80c and presents separation-of-function mutants that allow probing different mechanisms of Mps1 recruitment regulation. The findings show that the Ndc80c:Mps1 interface coincides with the binding site of the Dam1 C terminus, illuminating the mechanistic relationship between the error correction machinery and the SAC. Ipl1-controlled error correction promotes Mps1 binding by avoiding competition between Mps1 and Dam1 for Ndc80c, allowing sustained checkpoint signaling in prometaphase. The maturation of kinetochore end-on attachments is then coupled to SAC silencing via Dam1-dependent displacement of Mps1 from its kinetochore receptor binding site. The study also identifies that Mps1 autophosphorylation sites cluster in the Ndc80c binding interface. The results show that the described binding interface is sensitive to changes in Mps1 autophosphorylation, a hallmark of Mps1 kinetochore recruitment in many systems. The study further demonstrates that Dam1-dependent displacement regulates Mps1 binding to Ndc80c. Ipl1 phosphorylation of the Dam1 C terminus prevents Mps1 removal from Ndc80c. The findings highlight the importance of the Mps1-Ndc80c interface in kinetochore function and SAC signaling. The study provides a mechanistic explanation for the checkpoint silencing defect of the dam1 3D allele. The results suggest that the Dam1 C terminus cannot effectively compete with Mps1 for the binding site on Ndc80c in the dam1 3D mutant. The study also shows that the Mps1 kinetochore recruitment mechanism is fully compatible with simultaneous microtubule binding by Ndc80c. The findings exclude that direct binding competition between Mps1 and microtubules for Ndc8The study reveals how the kinase Mps1 is recruited to the kinetochore to enable mitotic checkpoint signaling. Upon formation of bi-oriented kinetochore-microtubule attachments, the Dam1 complex displaces Mps1 from its binding site on the Ndc80 complex, promoting anaphase onset. The N-terminal segment of Mps1 binds the neck region of Ndc80:Nuf2, the main microtubule receptor of kinetochores. Mutational disruption of this interface prevents Mps1 localization, eliminates SAC signaling, and impairs growth. The same interface of Ndc80:Nuf2 binds the Dam1 complex. The error correction kinase Ipl1 phosphorylates the Dam1 C terminus, preventing Dam1 from displacing Mps1 during error correction. The binding of the Dam1 complex to Ndc80:Nuf2 may release Mps1 from the kinetochore to promote anaphase onset. The study identifies the binding interface between Mps1 and Ndc80c and presents separation-of-function mutants that allow probing different mechanisms of Mps1 recruitment regulation. The findings show that the Ndc80c:Mps1 interface coincides with the binding site of the Dam1 C terminus, illuminating the mechanistic relationship between the error correction machinery and the SAC. Ipl1-controlled error correction promotes Mps1 binding by avoiding competition between Mps1 and Dam1 for Ndc80c, allowing sustained checkpoint signaling in prometaphase. The maturation of kinetochore end-on attachments is then coupled to SAC silencing via Dam1-dependent displacement of Mps1 from its kinetochore receptor binding site. The study also identifies that Mps1 autophosphorylation sites cluster in the Ndc80c binding interface. The results show that the described binding interface is sensitive to changes in Mps1 autophosphorylation, a hallmark of Mps1 kinetochore recruitment in many systems. The study further demonstrates that Dam1-dependent displacement regulates Mps1 binding to Ndc80c. Ipl1 phosphorylation of the Dam1 C terminus prevents Mps1 removal from Ndc80c. The findings highlight the importance of the Mps1-Ndc80c interface in kinetochore function and SAC signaling. The study provides a mechanistic explanation for the checkpoint silencing defect of the dam1 3D allele. The results suggest that the Dam1 C terminus cannot effectively compete with Mps1 for the binding site on Ndc80c in the dam1 3D mutant. The study also shows that the Mps1 kinetochore recruitment mechanism is fully compatible with simultaneous microtubule binding by Ndc80c. The findings exclude that direct binding competition between Mps1 and microtubules for Ndc8