A specific PP2A regulatory subunit, B56γ, mediates DNA damage‐induced dephosphorylation of p53 at Thr55

[1]  Gang Wei,et al.  Purification of acetyl-p53 using p300 co-infection and the baculovirus expression system. , 2005, Protein expression and purification.

[2]  C. van Hoof,et al.  PP2A: the expected tumor suppressor. , 2005, Current opinion in genetics & development.

[3]  F. McCormick,et al.  Role for PP2A in ARF signaling to p53. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[4]  R. Weinberg,et al.  Species- and cell type-specific requirements for cellular transformation. , 2004, Cancer cell.

[5]  H. Sheppard,et al.  Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for TAF1 in cell G1 progression. , 2004, Molecular cell.

[6]  W. Hahn,et al.  Identification of specific PP2A complexes involved in human cell transformation. , 2004, Cancer cell.

[7]  C. van Hoof,et al.  PP2A fulfills its promises as tumor suppressor: which subunits are important? , 2004, Cancer cell.

[8]  C. Whiteford,et al.  Phosphorylation of p53 at serine 37 is important for transcriptional activity and regulation in response to DNA damage , 2004, Oncogene.

[9]  D. Elliott,et al.  Expression of the B56δ subunit of protein phosphatase 2A and Mea1 in mouse spermatogenesis. Identification of a new B56γ subunit (B56γ4) specifically expressed in testis , 2004, Cytogenetic and Genome Research.

[10]  C. van Hoof,et al.  Phosphatases in apoptosis: to be or not to be, PP2A is in the heart of the question. , 2003, Biochimica et biophysica acta.

[11]  Y. Endo,et al.  A truncated isoform of the protein phosphatase 2A B56gamma regulatory subunit may promote genetic instability and cause tumor progression. , 2003, The American journal of pathology.

[12]  J. del Mazo,et al.  Expression of the B56delta subunit of protein phosphatase 2A and Mea1 in mouse spermatogenesis. Identification of a new B56gamma subunit (B56gamma4) specifically expressed in testis. , 2003, Cytogenetic and Genome Research.

[13]  Ronald A. DePinho,et al.  p53: good cop/bad cop. , 2002, Cell.

[14]  S. Thorgeirsson,et al.  Cyclin G recruits PP2A to dephosphorylate Mdm2. , 2002, Molecular cell.

[15]  J. Minna,et al.  Genomic Organization and Mapping of the Gene Encoding the PP2A B56γ Regulatory Subunit , 2002 .

[16]  J. Minna,et al.  Genomic organization and mapping of the gene encoding the PP2A B56gamma regulatory subunit. , 2002, Genomics.

[17]  A. Schönthal,et al.  Role of serine/threonine protein phosphatase 2A in cancer. , 2001, Cancer letters.

[18]  E. Sontag.  Protein phosphatase 2A: the Trojan Horse of cellular signaling. , 2001, Cellular signalling.

[19]  A. Levine,et al.  Surfing the p53 network , 2000, Nature.

[20]  A. Gatti,et al.  Phosphorylation of human p53 on Thr-55. , 2000, Biochemistry.

[21]  D. Virshup,et al.  Protein phosphatase 2A: a panoply of enzymes. , 2000, Current opinion in cell biology.

[22]  J. Levine,et al.  Surfing the p53 network , 2000, Nature.

[23]  K. Kinzler,et al.  Requirement for p53 and p21 to sustain G2 arrest after DNA damage. , 1998, Science.

[24]  D. Virshup,et al.  The B56 Family of Protein Phosphatase 2A (PP2A) Regulatory Subunits Encodes Differentiation-induced Phosphoproteins That Target PP2A to Both Nucleus and Cytoplasm* , 1996, The Journal of Biological Chemistry.

[25]  A. Brothman,et al.  Assignment of human protein phosphatase 2A regulatory subunit genes b56alpha, b56beta, b56gamma, b56delta, and b56epsilon (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12. , 1996, Genomics.

[26]  S. Durbin,et al.  High Complexity in the Expression of the B′ Subunit of Protein Phosphatase 2A0 , 1996, The Journal of Biological Chemistry.

[27]  N. Berndt,et al.  In vivo and in vitro binding of microcystin to protein phosphatases 1 and 2A. , 1995, Biochemical and biophysical research communications.

[28]  T. Yasumoto,et al.  Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: method of analysis of interactions of tight-binding ligands with target protein. , 1995, The Biochemical journal.

[29]  A. Deisseroth,et al.  Hyperphosphorylation of p53 induced by okadaic acid attenuates its transcriptional activation function. , 1994, Cancer research.

[30]  A. Komori,et al.  Hyperphosphorylation of retinoblastoma protein and p53 by okadaic acid, a tumor promoter. , 1993, Cancer research.

[31]  M. Mumby,et al.  Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen , 1991, Molecular and cellular biology.