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© The Rockefeller University Press, 0021-9525/1998//1207 $5.00
The Journal of Cell Biology, Volume 141, Number 5, , 1998 1207-1215

Differential Subcellular Localization of Protein Phosphatase-1 , 1, and Isoforms during Both Interphase and Mitosis in Mammalian Cells

Paul R. Andreassen^*, Françoise B. Lacroix^*, Emma Villa-Moruzzi, and Robert L. Margolis^*

^* Institut de Biologie Structurale Jean-Pierre Ebel (CEA-CNRS), 38027 Grenoble cedex 1, France; and Department of Biomedicine, University of Pisa, 56126 Pisa, Italy

Protein phosphatase-1 (PP-1) is involved in the regulation of numerous metabolic processes in mammalian cells. The major isoforms of PP-1, , 1, and , have nearly identical catalytic domains, but they vary in sequence at their extreme NH₂ and COOH termini. With specific antibodies raised against the unique COOH-terminal sequence of each isoform, we find that the three PP-1 isoforms are each expressed in all mammalian cells tested, but that they localize within these cells in a strikingly distinct and characteristic manner. Each isoform is present both within the cytoplasm and in the nucleus during interphase. Within the nucleus, PP-1 associates with the nuclear matrix, PP-1 1 concentrates in nucleoli in association with RNA, and PP-1 localizes to nonnucleolar whole chromatin. During mitosis, PP-1 is localized to the centrosome, PP-1 1 is associated with microtubules of the mitotic spindle, and PP-1 strongly associates with chromosomes. We conclude that PP-1 isoforms are targeted to strikingly distinct and independent sites in the cell, permitting unique and independent roles for each of the isoforms in regulating discrete cellular processes.

Abbreviations used in this paper: CENP-A, centromere protein-A; CREB, cAMP response element binding; PP-1, protein phosphatase-1.

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