Numerous cell processes are regulated via the dephosphorylation of key proteins by type-1 protein phosphatase (PP1) holoenzymes. In addition to the PP1 catalytic subunit, these holoenzymes contain one or more non-catalytic subunits that specify the localisation, activity and substrate affinity of the complex. This publication describes the characterisation of one such non-catalytic subunit, Sds22, which has been implicated in the regulation of mitosis. It reports on the genomic structure and the expression of the human and the mouse sds22-encoding gene and on the prediction of the three-dimensional structure of Sds22. Furthermore, it is discussed how determinants of Sds22 and of the catalytic subunit contribute to the interaction between the two proteins and to the functionality of Sds22.
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