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The molecular consequences of 14\u20103\u20103 binding are diverse: this binding may result in stabilization of the active or inactive phosphorylated form of the protein, to a conformational alteration leading to activation or inhibition, to a different subcellular localization, to the interaction with other proteins or to shielding of binding sites. The binding partners, and hence the 14\u20103\u20103 proteins, are involved in almost every cellular process and 14\u20103\u20103 proteins have been linked to several diseases, such as cancer, Alzheimer's disease, the neurological Miller\u2013Dieker and spinocerebellar ataxia type 1 diseases and bovine spongiform encephalopathy (BSE). The yeasts <jats:italic>Saccharomyces cerevisiae<\/jats:italic> and <jats:italic>Schizosaccharomyces pombe<\/jats:italic> both have two genes encoding 14\u20103\u20103 proteins, <jats:italic>BMH1<\/jats:italic> and <jats:italic>BMH2<\/jats:italic> and <jats:italic>rad24<\/jats:italic> and <jats:italic>rad25<\/jats:italic>, respectively. In these yeasts, 14\u20103\u20103 proteins are essential in most laboratory strains. As in higher eukaryotes, yeast 14\u20103\u20103 proteins bind to numerous proteins involved in a variety of cellular processes. Recent genome\u2010wide studies on yeast strains with impaired 14\u20103\u20103 function support the participation of 14\u20103\u20103 proteins in numerous yeast cellular processes. Given the high evolutionary conservation of the 14\u20103\u20103 proteins, the experimental accessibility and relative simplicity of yeasts make them excellent model organisms for elucidating the function of the 14\u20103\u20103 protein family. Copyright \u00a9 2006 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/yea.1338","type":"journal-article","created":{"date-parts":[[2006,2,24]],"date-time":"2006-02-24T11:18:11Z","timestamp":1140779891000},"page":"159-171","source":"Crossref","is-referenced-by-count":85,"title":["Yeast 14\u20103\u20103 proteins"],"prefix":"10.1002","volume":"23","author":[{"given":"G. 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