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Protein phosphatase 2A interacting proteins

This table lists proteins that have been shown to interact with PP2A. These interactions have been detected in a variety of ways including yeast two-hybrid assays, direct binding, and functional assays.

Protein Comments Refs
Adenomatous Polyposis Coli (APC) Binds to R5 subunits; may target PP2A to APC complex involved in regulating b-catenin levels and Wnt signaling pathway; overexpression of R5 decreases β-catenin levels 1, 2
Adenovirus E4orf4 protein Binds to AC-R2 complex; formation of complex required for E4orf4-mediated apoptosis 3, 4
Axin (Axin 1) Binds to C subunit; may target PP2A to a complex of axin, APC, GSK3, and β-catenin; suggests involvement in Wnt signaling pathway 2, 5
Bcl-2 Bcl-2 interacts with PP2A; PP2A dephosphorylates Bcl-2; may regulate function of Bcl-2 in apoptosis; dephosphorylation of Bcl-2 is stimulated by ceramide 6, 7
β-adrenergic receptor The β2-adrenergic receptor is a member of the G-protein coupled receptor family (GPCR). Association with PP2A is dependent on agonist stimulation, internalization, and acidification of endosomes. PP2A dephosphorylation of receptor is important for receptor resensitization and recycling to plasma membrane. 8
Biogenic amine transporters Dopamine, norepinephrine, and serotonin transporters associate with PP2A. Transporter phosphorylation results in disruption of the PP2A association. The interaction may be involved in the regulation of the surface expression of transporters. 53
E-cadherin
/β-catenin
The Cα, but not the Cβ catalytic subunit of PP2A is required for stabilization of E-cadherin/β-catenin complexes at the plasma membrane 46
Calcium channel (L-type, Cav1.2) PP2A binds to the pore-forming α1C subunit of this channel and reverses PKA-catalyzed serine phosphorylation. The interaction is selective for R5γ-containing PP2A complexes. 54
CaM kinase IV Binds to AC-R2 complex; substrate for C subunit of PP2A. Disrupting the interaction with SV40 small-t antigen in transfected cells alters CaMKIV-dependent activation of CREB transcription factor. 9
Cas
(p130 Crk-assoc substrate
Cas is a Src substrate that has increased association with PP2A when Src is activated. PP2A dephosphorylates serine residues on Cas in vitro. 45
Casein kinase 2 (CK2) CK2 binds to the AC dimer and stimulates phosphatase activity. 10
Caspase-3 Activates PP2A during apoptosis by proteolysis of the A subunit at a specific site. Enhanced dephosphorylation by PP2A may be important in apoptotic processes. 11
Cdc6 Cdc6 binds to R3/PR48 subunit; interacts with AC-PR48 complexes; may regulate DNA replication; overexpression of PR48 causes G1 arrest 12
Cdc25c Cdc25c was shown to co-immunoprecipitate with PP2A from cells treated with a cross-linking reagent. Interaction appears to require R2 subunits and results in dephosphorylation of cdc25c. Interaction is enhanced by HIV-1 Vpr protein. Dephosphorylation and inactivation of cdc25c could be an important mechanism in Vpr-mediated G2 arrest. 13
CG-NAP
(AKAP 350)
This 450-kDa centrosome and golgi localized PKN-associated protein coimmunoprecipitates with PP2A in R3α-130 expressing cells. CG-NAP is involved in regulation of centrosome dynamics during the cell cycle. 59
CXCR2
(chemokine receptor)
CXCR2 is a member of the CXC chemokine receptor family. These are G-protein coupled receptors (GPCRs) involved in chemotaxis of lymphcytes and neutrophils. CXCR2 interacts with the core dimer (AC) of PP2A. The interaction is dependent on internalization of receptor following agonist stimulation. 14
Cyclin G1 Cyclin G1 binds to R5 subunits and the association is dependent on the induction of p53. Cyclin G1 plays a role in enhancing apoptosis. 15
Cyclin G2 The association of cyclin G2 with PP2A catalytic and R5 subunits correlates with its ability to inhibit cell cycle progression. 51
DNA polymerase α primase PP2A is recovered with the hypophosphorylated form of DNA polymerase a-primase in G1. PP2A dephosphorylates DNA polymerase a-primase and restores its origin-dependent initiation activity in vito. 52
eRF1 Binds to AC dimer through C subunit; might target AC dimer to ribosomes 17
Estrogen receptorα ERα co-immunoprecipitates with PP2A activity. The PP2A catalytic subunit binds to ERα and dephosphorylates Ser118. 61
HSF2 HSF2 interacts with the A subunit in two-hybrid assay and co-immunoprecipitations. May displace C subunit from PP2A holoenzymes. 18, 19
HIV Vpr protein Binds to AC-R2 complex; mediates Vpr-induced G2 arrest; regulates nuclear Cdc25 dual-specificity phosphatase (NOTE: reference 21 has been retracted). 20, 21
HOX11 Binds to C subunit; inhibits phosphatase activity 22
HRX Binds PP2A through I2PP2A; commonly mutated in acute leukemias 23
I1PP2A (PHAP1, mapmodulin) Inhibitor of PP2A in vitro 24
I2PP2A (SET) Inhibitor of PP2A in vitro
I-κB kinase (IKK) γ subunit IKKγ interacts with PP2A as detected by co-immunoprecipitation and GST-fusion protein assays 60
JAK2 Transient association upon interleukin-11 stimulation of adipocytes 26
Kinase suppressor of Raf KSR interacts with the R2α-containing isoform of the PP2A holoenzyme.  
Mid-1 Mid-1 binds to the alpha 4 protein and forms a complex with the PP2A catalytic subunit. This interaction may regulate mid-1 bindng to microtubules and formation of the midline during the cell cycle. 60
Neurofilament proteins A, R2, and C subunits associate with NF proteins; PP2A appears to dephosphorylate some sites in all three NF proteins (NF-L, NF-M, and NF-H); dephosphorylation by PP2A promotes assembly of NF-L 27, 28
NMDA receptor PP2A forms a stable complex with NR3A subunit of the NMDA receptor. The association increases phosphatase activity and dephosphorylation of the NR1 subunit. Stimulation of the receptor leads to dissociation of PP2A and a reduction in phosphatase activity. 55
p107 p107 (an pRB-related protein) binds R3/PR59 subunit-containing holoenzyme; over-expression of R3/PR59 causes p107 dephosphorylation and G1 arrest. 29
p21-activated kinase (PAK1) PAK1 is a PP2A substrate 30
p70 S6 kinase p70 S6 kinase is a PP2A substrate 30, 31
PKCa The PP2A catalytic subunit co-immunoprecipitates with PKCa. PKCa is dephosphorylated by PP2A. This association may be involved in the regulation of mast cell IL-6 production. 56
PKCδ PKCd is a substrate for PP2A. 57
PKR (EIF2AK1, PRKR) PKR binds to and phosphorylates the R5α regulatory subunit. This functional interaction may alter the activity of the translation initiation factor eIF4. 16
Polyomavirus middle tumor antigen Binds to AC dimer; increases tyrosine phosphatase activity of PP2A 32, 33
Polyomavirus small tumor antigen Similar to polyoma small t; binds to AC dimer; increases tyrosine phosphatase activity of PP2A 32, 33
Raf-1 Raf-1 can be dephosphorylated by PP2A 34
RelA RelA interacts with the scaffold subunit of PP2A in vitro. The association may be transient since cross-linking is required to isolate the PP2A/RelA complex. RelA is dephosphorylated by PP2A in vitro. 47
Sex combs reduced (SCR) SCR is a Drosophila homeobox transcription factor that interacts with the Drosophila homolog of the R5 subunit. SCR is highly homologous to human and mouse homeobox 5 and 6 proteins (HOX5 and HOX6). 35
SG2NA Binds AC dimer, localized in nucleus, contains WD repeats, binds calmodulin, unknown function 36
Shc PP2A associates with the PTB domain of Shc in the basal state and dissociates in response to insulin- and EGF-induced tyrosine phosphorylation. Expression of SV40 small-t antigen also causes dissociation of this complex. 48
Sp1 The Sp1 transcription factor interacts with the catalytic subunit in dividing T lymphocytes. 49
Src PP2A binds to the SH2, SH3, and catalytic domains of Src. This interaction decreases Src tyrosine kinase activity. 58
STAT5 STAT5 associates with PP2A in an IL-3-dependent manner in the cytoplasm but not the nucleus. 50
Striatin Binds to AC dimer, localized in post-synaptic densities of neuronal dendrites, contains WD repeats, binds calmodulin, unknown function 36
SV40 small tumor antigen Binds to AC dimer; displaces R2 subunits; inhibits PP2A activity 32
Tap42/alpha 4 (IGBP1) Interacts directly with the C subunit; also binds to PP4 and PP6; reduces the activity of the C subunit. Yeast homologue (Tap42) phosphorylated by Tor kinase which enhances association with the C subunit. 37-42
TAU Binds to R2-containing trimers and is a good substrate for PP2A; TAU dephosphorylation promotes microtubule binding and stabiliztion 43
Tax The human T-lymphotropic retrovirus type-I transactivator Tax interacts via a tripartite protein interaction that also involves IKKγ. The association of Tax with this complex inhibits PP2A activity and enhances the activity of IKK. 60
Vimentin The AC-R2 complex associates with and dephosphorylates vimentin; association is mediated by R2; depletion of R2 by antisense RNA cause hyperphosphorylation of vimentin. 44

References

1.         Seeling,J.M., Miller,J.R., Gil,R., Moon,R.T., White,R., Virshup,D.M. (1999). Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science 283, 2089-2091.PubMed

2.         Virshup,D.M. (2000). Protein phosphatase 2A: a panoply of enzymes. Curr. Op. Cell Biol. 12, 180-185. PubMed

3.         Kleinberger,T., Shenk,T. (1993). Adenovirus E4orf4 protein binds to protein phosphatase 2A, and the complex down regulates E1A-enhanced junB transcription. J.Virol. 67, 7556-7560.PubMed

4.         Shtrichman,R., Sharf,R., Barr,H., Dobner,T., Kleinberger,T. (1999). Induction of apoptosis by adenovirus E4orf4 protein is specific to transformed cells and requires an interaction with protein phosphatase 2A. Proc. Natl. Acad.Sci. U.S.A. 96, 10080-10085. PubMed

5.         Hsu,W., Zeng,L., Costantini,F. (1999). Identification of a domain of axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J. Biol. Chem. 274, 3439-3445. PubMed

6.         Deng,X.M., Ito,T., Carr,B., Mumby,M., May,W.S. (1998). Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. J. Biol. Cem. 273, 34157-34163. PubMed

7.         Ruvolo,P.P., Deng,X., Ito,T., Carr,B.K., May,W.S. (1999). Ceramide induces bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A. J. Biol. Chem. 274, 20296-20300. PubMed

8.         Krueger,K.M., Daaka,Y., Pitcher,J.A., Lefkowitz,R.J. (1997). The role of sequestration in G protein-coupled receptor resensitization. Regulation of beta2-adrenergic receptor dephosphorylation by vesicular acidification. J. Biol. Chem. 272, 5-8. PubMed

9.         Westphal,R.S., Anderson,K.A., Means,A.R., Wadzinski,B.E. (1998). A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A. Science 280, 1258-1261. PubMed

10.       Heriche,J.K., Lebrin,F., Rabilloud,T., Leroy,D., Chambaz,E.M., Goldberg,Y. (1997). Regulation of protein phosphatase 2A by direct interaction with casein kinase 2a. Science 276, 952-955. PubMed

11.       Santoro,M.F., Annand,R.R., Robertson,M.M., Peng,Y.W., Brady,M.J., Mankovich,J.A., Hackett,M.C., Ghayur,T., Walter,G., Wong,W.W., Giegel,D.A. (1998). Regulation of protein phosphatase 2A activity by caspase-3 during apoptosis. J. Biol. Chem. 273, 13119-13128. PubMed

12.       Yan,Z., Fedorov,S.A., Mumby,M.C., Williams,R.S. (2000). PR48, a Novel Regulatory Subunit of Protein Phosphatase 2A, Interacts with Cdc6 and Modulates DNA Replication in Human Cells. Mol.Cell Biol. 20, 1021-1029.PubMed

13.       Hrimech,M., Yao,X.J., Branton,P.E., Cohen,E.A. (2000). Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A. EMBO J. 19, 3956-3967. PubMed

14.       Fan,G.H., Yang,W., Sai,J., Richmond,A. (2001). Phosphorylation-independent Association of CXCR2 with the Protein Phosphatase 2A Core Enzyme. J. Biol. Chem. 276, 16960-16968. PubMed

15.       Okamoto,K., Kamibayashi,C., Serrano,M., Prives,C., Mumby,M.C., Beach,D. (1996). p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A. Mol. Cell. Biol. 16, 6593-6602. PubMed

16.       Xu,Z., Williams,B.R. (2000). The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR. Mol. Cell. Biol. 20, 5285-5299.

17.       Andjelkovic,N., Zolnierowicz,S., Van Hoof,C., Goris,J., Hemmings,B.A. (1996). The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15, 7156-7167.

18.       Hong,Y.L., Sarge,K.D. (1999). Regulation of protein phosphatase 2A activity by heat shock transcription factor 2. J. Biol. Chem. 274, 12967-12970.

19.       Hong,Y.L., Lubert,E.J., Rodgers,D.W., Sarge,K.D. (2000). Molecular basis of competition between HSF2 and catalytic subunit for binding to the PR65/A subunit of PP2A. Biochem. Biophys. Res. Comm. 272, 84-89.

20.       Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P., Ozon,R. (1997). Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr. FEBS Lett. 401, 197-201.

21.       Hrimech,M., Yao,X.J., Branton,P.E., Cohen,E.A. (2000). Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A. EMBO J. 19, 3956-3967. (Retraction published in EMBO J. 21:3918, 2002).

22.       Kawabe,T., Muslin,A.J., Korsmeyer,S.J. (1997). Hox11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint. Nature 385, 454-458.

23.       Adler,H.T., Nallaseth,F.S., Walter,G., Tkachuk,D.C. (1997). HRX leukemic fusion proteins form a heterocomplex with the leukemia- associated protein SET and protein phosphatase 2A. J. Biol. Chem. 272, 28407-28414.

24.       Li,M., Makkinje,A., Damuni,Z. (1996). The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 271, 11059-11062.

25.       Li,M., Makkinje,A., Damuni,Z. (1996). Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 35, 6998-7002.

26.       Fuhrer,D.K., Yang,Y.C. (1996). Complex formation of JAK2 with PP2A, P13K, and Yes in response to the hematopoietic cytokine interleukin-11. Biochem.Biophys.Res.Comm. 224, 289-296.

27.       Saito,T., Shima,H., Osawa,Y., Nagao,M., Hemmings,B.A., Kishimoto,T., Hisanaga,S. (1995). Neurofilament-associated protein phosphatase 2A: its possible role in preserving neurofilaments in filamentous states. Biochemistry 34, 7376-7384.

28.       Strack,S., Westphal,R.S., Colbran,R.J., Ebner,F.F., Wadzinski, B.E. (1997). Protein serine/threonine phosphatase 1 and 2A associate with and dephosphorylate neurofilaments. Brain Res. Mol.Brain Res. 49, 15-28.

29.       Voorhoeve,P.M., Hijmans,E.M., Bernards,R. (1999). Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein. Oncogene 18, 515-524.

30.       Westphal,R.S., Coffee,R.L., Marotta,A., Pelech,S.L., Wadzinski,B.E. (1999). Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J. Biol. Chem. 274, 687-692.

31.       Peterson,R.T., Desai,B.N., Hardwick,J.S., Schreiber,S.L. (1999). Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycin-associated protein. Proc. Natl. Acad. Sci. U.S.A. 96, 4438-4442.

32.       Mumby,M. (1995). Regulation by tumour antigens defines a role for PP2A in signal transduction. Sem.Cancer Biol. 6, 229-237.

33.       Cayla,X., Ballmer-Hofer,K., Merlevede,W., Goris,J. (1993). Phosphatase 2A associated with polyomavirus small-T or middle- T antigen is an okadaic acid-sensitive tyrosyl phosphatase. Eur. J. Biochem. 214, 281-286.

34.       Abraham,D., Podar,K., Pacher,M., Kubicek,M., Welzel,N., Hemmings,B.A., Dilworth,S.M., Mischak,H., Kolch,W., Baccarini,M. (2000). Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation. J. Biol. Chem. 275, 22300-22304.

35.       Berry,M., Gehring,W. (2000). Phosphorylation status of the SCR homeodomain determines its functional activity: essential role for protein phosphatase 2A-B’. EMBO J. 19, 2946-2957.

36.       Moreno,C.S., Park,S., Nelson,K., Ashby,D., Hubalek,F., Lane,W.S., Pallas,D.C. (2000). WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. J. Biol. Chem. 275, 5257-5263.

37.       DiComo,C.J., Arndt,K.T. (1996). Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 10, 1904-1916.

38.       Murata,K., Wu,J., Brautigan,D.L. (1997). B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc.Natl. Acad.Sci.U.S.A. 94, 10624-10629.

39.       Chen,J., Peterson,R.T., Schreiber,S.L. (1998). Alpha 4 associates with protein phosphatases 2A, 4, and 6. Biochem. Biophys. Res. Comm. 247, 827-832.

40.       Maeda,K., Inui,S., Tanaka,H., Sakaguchi,N. (1999). A new member of the alpha 4-related molecule (alpha 4-b) that binds to the protein phosphatase 2A is expressed selectively in the brain and testis. Eur. J. Biochem. 264, 702-706.

41.       Nanahoshi,M., Nishiuma,T., Tsujishita,Y., Hara,K., Inui,S., Sakaguchi,N., Yonezawa,K. (1998). Regulation of protein phosphatase 2A catalytic activity by alpha4 protein and its yeast homolog tap42. Biochem. Biophys. Res. Comm. 251, 520-526.

42.       Jiang,Y., Broach,J.R. (1999). Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast. EMBO J. 18, 2782-2792.

43.       Sontag,E., Nunbhakdi-Craig,V., Lee,G., Bloom,G.S., Mumby,M.C. (1996). Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A. Neuron 17, 1201-1207.

44.       Turowski,P., Myles,T., Hemmings,B.A., Fernandez,A., Lamb,N.C. (1999). Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol. Biol. Cell 10, 1997-2015.

45.      Yokoyama,N., Miller,W.T. (2001). Protein phosphatase 2A interacts with the Src kinase substrate p130(CAS). Oncogene 20, 6057-6065.

46.       Gotz,J, Probst,A. Mistl,C., Nitsch,R.M., Ehler,E. (2000). Distinct role of the protein phosphatase 2A subunit Ca in the regulation of E-cadherin and b-catenin during development. Mech. Devel. 93, 83-93.

47.       Yang,J., Fan,G.H., Wadzinski,B.E., Sakurai,H., A. Richmond. (2001). Protein phosphatase 2A interacts with and directly dephosphorylates RelA. J. Biol. Chem. 276, 47828-47833.

48.       Ugi, S., Imamura,T., Ricketts,W., Olefsky,J. M.. (2002). Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling. Mol. Cell. Biol. 22, 2375-2387.

49.       Lacroix,I., Lipcey,C., Imbert,J., Kahn-Perles,B. (2002). Sp1 transcriptional activity is up-regulated by phosphatase 2A in dividing T lymphocytes. J.Biol.Chem. 277, 9598-9605.

50.       Yokoyama,N., Reich,N.C., Miller W. T. (2001). Involvement of protein phosphatase 2a in the interleukin-3-stimulated jak2-stat5 signaling pathway. J.Interferon Cytokine Res. 21, 369-378.

51.       Bennin,D.A., Arachchige Don,A.S., Brake,T., McKenzie,J.L., Rosenbaum,H., Ortiz,L., DePaoli-Roach,A.A., Horne,M.C. (2002). Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B' subunits in active complexes and induces nuclear aberrations and a G1/S phase cell cycle arrest. J. Biol. Chem. 277, 27449-27467.

52.       Dehde,S., Rohaly,G., Schub,O., Nasheue,H.P., Bohn,W., Chemnitz,J., Deppert,W., Dornreiter,I. (2001). Two immunologically distinct human DNA polymerase alpha-primase subpopulations are involved in cellular DNA replication. Mol. Cell. Biol. 21, 2581-2593.

53.       Bauman,A.L., Apparsundaram,S., Ramamoorthy,S., Wadzinski,B.E., Vaughan,R.A., Blakely,R.D. (2000). Cocaine and antidepressant-sensitive biogenic amine transporters exist in regulated complexes with protein phosphatase 2A. J. Neurosci. 20:7571-7578. PubMed.

54.       Davare,M.A., Horne,M.C., Hell,J.W. (2000). Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP- dependent protein kinase. J. Biol. Chem. 275, 39710-39717.

55.       Chan,S.F., Sucher,N.J. (2001). An NMDA receptor signaling complex with protein phosphatase 2A. J. Neurosci. 21, 7985-7992.

56.       Boudreau,R.T., Garduno,R., and Lin,T.J. (2002). Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells. J. Biol. Chem. 277, 5322-5329.

57.       Srivastava, J., Goris,J., Dilworth,S.M., Parker,P.J. (2002). Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides. FEBS Lett. 516, 265-269.

58.       Yokoyama,N., Miller,W.T. (2001). Inhibition of Src by direct interaction with protein phosphatase 2A. FEBS Lett. 505, 460-464.

59.       Takahashi, M., Shibata,H., Shimakawa,M., Miyamoto,M., Mukai,H., Ono,Y.. (1999). Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus. J. Biol. Chem. 274, 17267-17274.

60.       Fu, D.-X., Kuo, Y.-L., Liu, B.-Y., Jeang, R.-T., and Giam, C.-Z. (2003). Human T-lymphotrophic virus type I Tax activates I-kB kinase by inihibiting I-kB kinase associated serine/threonine protein phosphatase 2A. J. Biol. Chem. 278, 1487-1493.

61.       Lu, Q., Surks, H.K., Ebling, H., Baur, W.E., Brown, D., Pallas, D.C., and Karas, R.H. (2003). Regulation of estrogen receptor a mediated transcription by a direct interaction with protein phosphatase 2A. J. Biol. Chem. 278, 4639-4645. PubMed.