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IN BRIEF

PASTICCINO2 Antiphosphatase: Balancing Cell Division and Differentiation

neckardt{at}aspb.org

Protein Tyr phosphatase (PTP)-like proteins are a highly conserved protein family in eukaryotes characterized by an inactive phosphatase domain. They have essential cellular functions in yeast and mammals, but their precise role in cellular metabolism is unknown. Da Costa et al. (pages 1426–1437) investigate the Arabidopsis PTP-like protein PASTICCINO2 (PAS2) and show that it interacts with cyclin-dependent kinase (CDK) that is phosphorylated on Tyr and not with its unphosphorylated isoform. Loss of PAS2 function in Arabidopsis resulted in dephosphorylation of CDKA;1 and upregulated its kinase activity. This suggests that PAS2, like other PTP-like proteins, functions as an antiphosphatase that binds substrate and prevents its dephosphorylation by other phosphatases. Overexpression of the protein showed that PAS2 acts as a repressor at the G2-to-M transition and as a potent factor maintaining cells in a differentiated state. PAS2 was localized in the cytoplasm of dividing cells but moved into the nucleus upon cell differentiation, suggesting that the balance between cell division and differentiation depends on the interaction between CDKA;1 and the antiphosphatase PAS2.

View larger version (64K): [in this window] [in a new window]   PAS2:GFP localized mainly outside the nucleus in interphase cells (left) and tightly associated with chromosomes during mitosis (right).

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Arabidopsis PASTICCINO2 Is an Antiphosphatase Involved in Regulation of Cyclin-Dependent Kinase A

Marco Da Costa, Liên Bach, Isabelle Landrieu, Yannick Bellec, Olivier Catrice, Spencer Brown, Lieven De Veylder, Guy Lippens, Dirk Inzé, and Jean-Denis Faure
Plant Cell 2006 18: 1426-1437. [Abstract] [Full Text]  

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