Inactivation of the master mitotic checkpoint regulator Mps1 by protein phosphatase 1 is required for timely segregation of the genetic material during cell division.

Cytological analyses combined with in vitro liposome reconstitution reveal that yeast SUN domain protein, Mps3, shows meiosis-specific phosphorylation in the luminal region of the nuclear envelope during meiosis for chromosome motion and nuclear envelope remodelling.

Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.

Visualization of yeast spindle pole proteins using a new microscopy method shows that assembly into the nuclear membrane occurs at the same time as duplication.

Msp1 recruits substrates at the open seam of the spiral oligomer and extracts them with functionally adapted elements.

Humans with mutations in the AIRE gene exhibit common autoantibodies targeting ovarian and intestinal antigens, including intestinal dysfunction-associated antibodies to enteroendocrine transcription factor RFX6.

Interacting MKS1 and UBE2E1 regulate canonical Wnt signaling through modulation of beta-catenin levels at the base of primary cilium, providing new insights into ciliopathy disease mechanisms.

PS1 phosphorylation at Ser367 is the potential hyperactivity-driven culprit of pathogenic change in PS1 conformation in vitro and in vivo.

The spindle checkpoint kinase Mps1 sequentially phosphorylates multiple substrates to amplify checkpoint signals, making the checkpoint highly dependent on Mps1 function and directly responsive to kinetochore-microtubule attachment.

Chromosomal instability induced in solid tumors can combine with macrophages that are made highly phagocytic to thereby initiate elimination of and immunity against poorly immunogenic tumors in immunocompetent mice.