Interaction of maize [Zea mays] protein phosphatase 2A with tubulin

• Autorzy: Awotunde O. S. , Lechward K. , Krajewska K. , Zolnierowicz S. , Muszynska G.
• Języki publikacji: EN

Abstrakty

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-a-tubulin anti­body. The interaction of plant PP2A with tubulin indicates a possible role of reversible protein phosphorylation in the dynamic structure of plant cytoskeleton.

Słowa kluczowe

EN

Zea mays; cytoskeleton organization; protein-protein interaction; tubulin; protein phosphatase 2A; maize; plant

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 1
• Opis fizyczny: p.131-138,fig.

Twórcy

autor

Awotunde O. S.

• Polish Academy of Sciences, A.Pawinskiego 5A, 02-106 Warsaw, Poland

autor

Lechward K.

autor

Krajewska K.

autor

Zolnierowicz S.

autor

Muszynska G.

Bibliografia

• Arino J, Perez-Callejon E, Cunillera N, Camps M, Posas F, Ferres A. (1993) Protein phosphatases in higher plants: multiplicity of type 2A phosphatases in Arabidopsis thaliana. PlantMolBiol.; 21: 475-85.
• Awotunde OS, Sugajska E, Zolnierowicz S, Muszynska G. (2000) Characterisation of two protein phosphatase 2A holoenzymes from maize seedlings. Biochim Biophys Acta.; 1480: 65-76.
• Ayaydin F, Vissi E, Meszaros T, Miskolczi P, Kovacs I, Feher A, Dombradi V, Erdodi F, Gergely P, Dudits D. (2000) Inhibition of serine/threonine-specific protein phosphatases causes premature activation of cdc2MsF kinase at G2/M transition and early mitotic microtubule organisation in alfalfa. Plant J.; 23: 85-96.
• Baskin TI, Wilson JE. (1997) Inhibitors of protein kinases and phosphatases alter root morphology and disorganize cortical microtubules. Plant Physiol.; 113: 493-502.
• Bradford MM. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem.; 72: 248-54.
• Cassimeris L. (2002) The oncoprotein 18/stathmin family of microtubule destabilizers. Curr Opin Cell Biol.; 14: 18-24.
• Deruere J, Jackson K, Garbers C, Soll D, DeLong A. (1999) The RCN1-encoded A subunit of protein phosphatase 2A increases phosphatase activity in vivo. Plant J.; 20: 389-99.
• Evans DRH, Stark MJR. (1997) Mutations in the Saccharomyces cerevisiae type 2A protein phosphatase catalytic subunit reveal roles in cell wall integrity, actin cytoskeleton organization and mitosis. Genetics.; 145: 227-41.
• Hiraga A, Tamura S. (2000) Protein phosphatase 2A is associated in an inactive state with microtubules through 2A1- specific interaction with tubulin. Biochem J.; 346: 433-9.
• Hunt AJ, McIntosh JR. (1998) The dynamic behavior of individual microtubules associated with chromosomes in vitro. Mol Biol Cell.; 9: 2857-71.
• Janssens V, Goris J. (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling. Biochem J.; 353: 417-39.
• Kinoshita K, Nemoto T, Nabeshima K, Kondoh H, Niwa H, Yanagida M. (1996) The regulatory subunits of fission yeast protein phosphatase 2A (PP2A) affect cell morphogenesis, cell wall synthesis and cytokinesis. Genes Cells.; 1: 29-45.
• Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriphage T4. Nature.; 227: 680-5.
• Lechward K, Awotunde OS, Swiatek W, Muszynska G. (2001) Protein phosphatase 2A: variety of forms and diversity of functions. Acta Biochim Polon.; 48: 921-33.
• MacKintosh C, Cohen P. (1989) Identification of high levels of type 1 and type 2A protein phosphatases in higher plants. Biochem J.; 262: 335-9.
• MacKintosh RW, Haycox G, Hardie DG, Cohen PTW. (1990) Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett ; 276: 156-60.
• Merrick SE, Demoise DC, Lee VM-Y. (1996) Site-specific dephosphorylation of tau protein at Ser202/Thr205 in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A. J Biol Chem.; 271: 5589-94.
• Nick P, Lambert A-M, Vantard M. (1995) A microtubule-associated protein in maize is expressed during phytochrome- induced cell elongation. Plant J.; 8: 835-44.
• Shibaoka H. (1991) In: The cytoskeletal basis ofplant growth and form.. pp 159-68. Lloyd CW. ed, Academic Press, London.
• Smith RD, Wilson JE, Walker JC, Baskin TI. (1994) Protein-phosphatase inhibitors block root hair growth and alter cortical cell shape of Arabidopsis roots. Planta.; 194: 516-24.
• Snaith HA, Armstrong CG, GuoY, Kaiser K, Cohen PTW. (1996) Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachments of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos. J. Cell Sci.; 109: 3001-12.
• Sontag E, Nunbhakdi-Craig V, Bloom GS. Mumby MC. (1995) A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol.; 128: 1131-44.
• Sontag E, Nunbhadki-Craig V, Lee G, Brandt R, Kamibayashi C, Kuret J, White III CL, Mumby MC, Bloom GS. (1999) Molecular interactions among protein phosphatase 2A, tau, and microtubules. J Biol Chem. ; 274: 25490-8.
• Tournebize R, Andersen SSL, Verde F, Doree M, Karsenti E, Hyman AA. (1997) Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis. EMBO J.; 16: 5537-49.
• Uribe X, Torres MA, Capellades M, Puigdomenech P, Rigau J. (1998) Maize alpha-tubulin genes are expressed according to specific patterns of cell differentiation. Plant Mol Biol. ; 37: 1069-78.