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  4. PI3K/Akt結合パートナー表

PI3K/Akt結合パートナー表

結合パートナー結合の影響Akt活性への影響参考文献
GAPDH活性化したAktと結合し、その脱リン酸化を制限促進Jacquin, M.A. et al. (2013) Cell Death Differ. 20, 1043–1054.
Jade-1結合してAktキナーゼ活性を阻害抑制Zeng, L. et al. (2013) Cancer Res. 73, 5371–5380.
Mst1結合してAktキナーゼ活性を阻害抑制Cinar, B. et al. (2007) EMBO J. 26, 4523–4534.
Jang, S.W. et al. (2007) J. Biol. Chem. 282, 30836–30844.
ArgBP2γ結合して、AktとPAK1のアダプターとして機能N/AYuan, Z.Q. et al. (2005) J. Biol. Chem. 280, 21483–21490.
CBPAktはCBPと結合してリン酸化し、CBP活性を調節N/ALiu, Y. et al. (2013) FEBS Lett. 587, 847–853.
PP1Aktと結合し、AktのThr450を脱リン酸化抑制Xiao, L. et al. (2010) Cell Death Differ. 17, 1448–1462.
PLCγ1AktはPLCγ1と結合してリン酸化N/AWang, Y. et al. (2006) Mol. Biol. Cell 17, 2267–2277.
Skp2AktはSkp2と結合してリン酸化し、Skp2活性を調節N/ALin, H. et al. (2009) Nat. Cell Biol. 11, 420–432.
Gao, D. et al. (2009) Nat. Cell Biol. 11, 397–408
PEA-15AktはPEA-15と結合してリン酸化し、抗アポトーシス機能を制御N/ATrencia, A. et al. (2003) Cell. Biol. 23, 4511–4521.
PHF20AktはPHF20と結合してリン酸化し、細胞内局在を制御N/APark, S. et al. (2012) J. Biol. Chem. 287, 11151–11163. 
PHLPPPHLPPはAktに結合し、AktのSer473を脱リン酸化抑制Gao, T. et al. Mol. Cell 18, 13–24.
FKBP5Aktと結合し、PHLPPとのAktの相互作用の足場として機能抑制Pei, H. et al. (2009) Cancer Cell 16, 259–266. 
CKIP-1Aktと結合し、Akt リン酸化を阻害抑制Tokuda, E. et al. (2007) Cancer Res. 67, 9666–9676.
RasAktのPH (pleckstrin homology) ドメインと相互作用促進Yue, Y. et al. (2004) J. Biol. Chem. 279, 12883–12889. 
BTBD10Aktと結合し、脱リン酸化を阻害促進Nawa, M. et al. (2008) Cell Signal. 20, 493–505.
KCTD20Aktと結合し、脱リン酸化を阻害促進Nawa, M. et al. (2013) BMC Biochem. 14, 27.
PAR-4AktはPAR-4と結合してリン酸化し、アポトーシス促進性活性を阻害N/AGoswami, A. et al. (2005) Mol. Cell 20, 33–44.
Tpl2AktはTpl2と結合してリン酸化N/AKane, L.P. et al. (2002) Mol. Cell. Biol. 22, 5962–5974.
SirT2SirT2はAktと相互作用し、Aktの適切な活性化に必要促進Ramakrishnan, G. et al. (2014) J. Biol. Chem. 289, 6054–6066. 
NPMAktのPH (Pleckstrin domain) に結合し、細胞生存を促進N/ALee, S.B. et al. (2008) Proc. Natl. Acad. Sci. USA 105, 16584–16589.
Kwon, I.S. et al. (2010) BMB Rep. 43, 127–132.
eEF1AAktと相互作用し、Aktリン酸化に寄与促進Pecorari, L. et al. (2009) Mol. Cancer 8, 58.
CLIPR-59Aktのキナーゼドメインと相互作用し、Aktの細胞内局在を調節N/ADing, J. et al. (2009) Mol. Cell. Biol. 29, 1459–1471. 
CNK1結合してAkt活性を増強促進Fritz, R.D. et al. (2010) Oncogene 29, 3575–3582.
Phafin2リソソームでAktと結合し、オートファジーを調節N/AMatsuda–Lennikov, M. et al. (2014) PLoS One 9, e79795. 
BtkAktと結合し、Aktのリン酸化を促進促進Lindvall, J. et al. (2002) Biochem. Biophys. Res. Commun. 293, 1319–1326.
β-ParvinAktと結合し、ILKとAktとの相互作用を妨害抑制Kimura, M. et al. (2010) J. Cell Sci. 123, 747–755. 
NS1AktのPH (pleckstrin homology) ドメインと相互作用促進Matsuda, M. et al. (2010) Biochem. Biophys. Res. Commun. 395, 312–317. 
α-SynucleinAktと結合し、Akt活性化を促進促進Chung, J.Y. et al. (2011) Neurosignals 19, 86–96. 
RACK1RACK1は、PP2Aとの複合体でAktと相互作用抑制Li, G. et al. (2012) Nat. Commun. 3, 667.
ProFAktと結合し、Aktの細胞内局在に影響N/AFritzius, T. et al. (2006) Biochem. J. 399, 9–20.
p27 Kip1Aktはp27と結合してリン酸化N/ALiang, J. et al. (2002) Nat. Med. 8, 1153–1160.
Shin, I. et al. (2002) Nat. Med. 8, 1145–1152.
FoxA2/HNF3βAktはFoxA2/HNF3βと結合してリン酸化N/AWolfrum, C. et al. (2003) Proc. Natl. Acad. Sci. USA 100, 11624–11629. 
DNMT1AktはDNMT1と結合してリン酸化N/AEstève, P.O. et al. (2011) Nat. Struct. Mol. Biol. 18, 42–48.

CSTはこの表を作成してくださった、ヨーク大学のMichael Scheid博士 (オンタリオ州トロント) に感謝いたします。

参考文献

  1. Ding, Z. et al. (2006) A retrovirus-based protein complementation assay screen reveals functional AKT1-binding partners. Proc. Natl. Acad. Sci. U.S.A. 103, 15014–15019.
  2. Lin, H.K. et al. (2002) Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J. 21, 4037–4048.
  3. Anai, M. et al. (2005) A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis. J. Biol. Chem. 280, 18525–18535.
  4. Mitsuuchi, Y. et al. (1999) Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2. Oncogene 18, 4891–4898.
  5. Zhang, P. et al. (2005) Regulated association of protein kinase B/Akt with breast tumor kinase. J. Biol. Chem. 280, 1982–1991.
  6. Fuhrmann, G. et al. (2001) Cdc25A phosphatase suppresses apoptosis induced by serum deprivation. Oncogene 20, 4542–4553.
  7. Miyata, Y. et al. (2004) CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 24, 4065–4074.
  8. Maira, S.M. et al. (2001) Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane. Science 294, 374–380.
  9. Bauer, P.M. et al. (2003) Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase. J. Biol. Chem. 278, 14841–14849.
  10. Remy, I. et al. (2004) Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt. Mol. Cell. Biol. 24, 1493–1504.
  11. Jahn, T. et al. (2002) Role for the adaptor protein Grb10 in the activation of Akt. Mol. Cell. Biol. 22, 979–991.
  12. Rane, M.J. et al. (2003) Heat shock protein 27 controls apoptosis by regulating Akt activation. J. Biol. Chem. 278, 27828–27835.
  13. Persad, S. et al. (2001) Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 276, 27462–27469.
  14. Cenni, V. et al. (2003) Interleukin-1-receptor-associated kinase 2 (IRAK2)-mediated interleukin-1-dependent nuclear factor kappaB transactivation in Saos2 cells requires the Akt/protein kinase B kinase. Biochem. J. 376, 303–311.
  15. Kim, A.H. et al. (2002) Akt1 regulates a JNK scaffold during excitotoxic apoptosis. Neuron 35, 697–709.
  16. Héron-Milhavet, L. et al. (2006) Only Akt1 is required for proliferation, while Akt2 promotes cell cycle exit through p21 binding. Mol. Cell. Biol. 26, 8267–8280.
  17. van den Heuvel, A.P. et al. (2002) Binding of protein kinase B to the plakin family member periplakin. J. Cell. Sci. 115, 3957–3966.
  18. Ahn, J.Y. et al. (2004) PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion. J. Biol. Chem. 279, 16441–16451.
  19. Pim, D. et al. (2005) Activation of the protein kinase B pathway by the HPV-16 E7 oncoprotein occurs through a mechanism involving interaction with PP2A. Oncogene 24, 7830–7838.
  20. Figueroa, C. et al. (2003) Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex. J. Biol. Chem. 278, 47922–47927.
  21. Sun, L. et al. (2004) Akt binds prohibitin 2 and relieves its repression of MyoD and muscle differentiation. J. Cell. Sci. 117, 3021–3029.
  22. Reusch, H.P. et al. (2001) Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells. J. Biol. Chem. 276, 33630–33637.
  23. Conery, A.R. et al. (2004) Akt interacts directly with Smad3 to regulate the sensitivity to TGF-beta induced apoptosis. Nat. Cell Biol. 6, 366–372.
  24. Remy, I. et al. (2004) PKB/Akt modulates TGF-beta signalling through a direct interaction with Smad3. Nat. Cell Biol. 6, 358–365.
  25. Laine, J. et al. (2000) The protooncogene TCL1 is an Akt kinase coactivator. Mol. Cell 6, 395–407.
  26. Pekarsky, Y. et al. (2000) Tcl1 enhances Akt kinase activity and mediates its nuclear translocation. Proc. Natl. Acad. Sci. U.S.A. 97, 3028–3033.
  27. Du, K. et al. (2003) TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science 300, 1574–1577.

作成日：2007年9月

改訂日：2014年9月