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Protein phosphatase 2A: Variety of forms and diversity of functions

100%
Lechward K., Awotunde O. S., Świątek W., Muszyńska G.
Acta Biochimica Polonica
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2001
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vol. 48
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issue 4
921-933
EN
Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine-and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A associates with regulatory proteins, termed variable subunits, in order to form trimeric holoenzymes attributed with distinct substrate specificity and targeted to different subcellular compartments. PP2Ac activity can be modulated by reversible phosphorylation on Tyr307 and methylation on C-terminal Leu309. Studies on PP2A have shown that this enzyme may be implicated in the regulation of metabolism, transcription, RNA splicing, translation, differentiation, cell cycle, oncogenic transformation and signal transduction.
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Interaction of maize (Zea mays) protein phosphatase 2A with tubulin

88%
Awotunde O. S., Lechward K., Krajewska K., Żołnierowicz S., Muszyńska G.
Acta Biochimica Polonica
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2003
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vol. 50
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issue 1
131-138
EN
Immunological and biochemical evidence has been obtained for an interaction of maize protein phosphatase 2A (PP2A) holoenzyme with tubulin. Tubulin co-purifies with maize seedling PP2A. Affinity chromatography of the maize PP2A preparation on immobilized tubulin revealed two peaks of phosphorylase a phosphatase activity. In one of the peaks, the catalytic (C) and constant regulatory (A) subunits of PP2A were identified by Western blotting. The subunits (C and A) of PP2A were co-immunoprecipitated from maize seedlings homogenate by an anti-α-tubulin antibody. The interaction of plant PP2A with tubulin indicates a possible role of reversible protein phosphorylation in the dynamic structure of plant cytoskeleton.
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