High impact information on NUD1

• Both functions of Nud1p are connected to the ability of Spc72p to bind to the outer plaque and half-bridge (via Kar1p) of the SPB [1].
• Here we analyze the function of Nud1p during yeast meiosis [1].
• Nud1p, a protein homologous to the mammalian centrosome and midbody component Centriolin, is a component of the budding yeast spindle pole body (SPB), with roles in anchorage of microtubules and regulation of the mitotic exit network during vegetative growth [1].
• The Nud1p-like domain of centriolin binds Bub2p, another component of the budding yeast pathway [2].
• The astral microtubule organizing function of Nud1p is mediated by its interaction with the gamma-tubulin complex binding protein Spc72p [3].

Biological context of NUD1

• Our results have allowed the identification of the first single amino acid mutation in NUD1, and suggest a link between cell cycle progression and cellular integrity [4].
• Another approach, in which classic genetic methods were combined with the use of yeast artificial chromosomes and traditional cloning procedures, allowed the identification of the NUD1 gene--which codes for a component of the spindle-pole body-as the wild-type gene corresponding to the ts4 mutation [4].
• Nud1p links astral microtubule organization and the control of exit from mitosis [3].
• Saccharomyces cerevisiae NUD1 gene codes for a spindle pole body component and nud1 temperature-sensitive mutants arrest at 38 degrees C in late anaphase with a tendency for lysis [5].
• The data show that the phenotype of S. cerevisiae nud1 mutants is characterized by enhanced export of secretory proteins and that the passage of proteins through the walls of nud1 cells is an active process [5].

Other interactions of NUD1

• Temperature-sensitive mutants for two of the components, Spc29p and Nud1p, were prepared to partly define their function [6].
• We have determined that this S. pombe Nud1p homolog corresponds to Cdc11p, a previously uncharacterized SIN element [7].

References