Protein phosphorylation is one of the main mechanisms by which signals are transmitted in eukaryotic cells, and it plays a crucial regulatory role in almost all cellular processes. In yeast, more than half of the proteins are phosphorylated in at least one site, and over 20,000 phosphopeptides have been experimentally verified. However, the functional consequences of these phosphorylation events for most of the identified phosphosites are unknown. A family of protein interaction domains selectively recognises phosphorylated motifs to recruit regulatory proteins and activate signalling pathways. Nine classes of dedicated modules are coded by the yeast genome: 14-3-3, FHA, WD40, BRCT, WW, PBD, and SH2. The recognition specificity relies on a few residues on the target protein and has coevolved with kinase specificity. In the present study, we review the current knowledge concerning yeast phospho-binding domains and their networks. We emphasise the relevance of both positive and negative amino acid selection to orchestrate the highly regulated outcomes of inter- and intra-molecular interactions. Finally, we hypothesise that only a small fraction of yeast phosphorylation events leads to the creation of a docking site on the target molecule, while many have a direct effect on the protein or, as has been proposed, have no function at all.

蛋白质磷酸化是真核细胞中信号传递的主要机制之一，它在几乎所有细胞过程中都起着至关重要的调节作用。在酵母中，一半以上的蛋白质在至少一个位点被磷酸化，并且已通过实验验证了超过20,000个磷酸肽。但是，这些磷酸化事件对大多数鉴定出的磷酸位点的功能后果尚不清楚。蛋白质相互作用域家族选择性识别磷酸化基序，以募集调节蛋白并激活信号传导途径。酵母基因组编码了九类专用模块：14-3-3，FHA，WD40，BRCT，WW，PBD和SH2。识别特异性依赖于靶蛋白上的一些残基，并且已经与激酶特异性共同发展。在目前的研究中，我们回顾了有关酵母磷酸结合域及其网络的当前知识。我们强调正氨基酸和负氨基酸选择的相关性，以协调分子间和分子间相互作用的高度调控的结果。最后，我们假设只有一小部分的酵母磷酸化事件会导致在靶分子上形成一个停靠位点，而许多对蛋白质有直接影响，或者完全没有作用。