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Gene Review

PLEKHO1  -  pleckstrin homology domain containing,...

Homo sapiens

Synonyms: C-Jun-binding protein, CK2-interacting protein 1, CKIP-1, CKIP1, Casein kinase 2-interacting protein 1, ...
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Disease relevance of PLEKHO1


High impact information on PLEKHO1


Biological context of PLEKHO1

  • During apoptosis, CKIP-1 is cleaved by caspase-3 and translocated to the cytoplasm and then to the nucleus [3].
  • Importantly, similar to Nmi and contrast to IFP35, CKIP-1 inhibits tumor cell growth and Akt-mediated cell survival [4].
  • Collectively, our data supports a model whereby CKIP-1 is a non-enzymatic regulator of CK2alpha that regulates the cellular functions of CK2alpha by targeting or anchoring CK2alpha to specific cellular localization or by functioning as an adapter to integrate CK2alpha-mediated signaling events with components of other signal transduction pathways [5].

Anatomical context of PLEKHO1


Physical interactions of PLEKHO1

  • Interestingly, CKIP-1 is localized both at the plasma membrane and in the nucleus dependent on the cell types, and only the plasma membrane-localized CKIP-1 could form a complex with ATM [2].
  • The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling [4].

Other interactions of PLEKHO1

  • Importantly, CKIP-1 recruits nuclear ATM proteins partially to the plasma membrane [2].
  • CKIP-1 (casein kinase-2 interacting protein-1) is implicated in muscle differentiation, regulation of cell morphology and actin cytoskeleton [2].
  • In this study, we present evidence from deletion analysis of CKIP-1 suggesting that a C-terminal region containing a putative leucine zipper has a role in regulating its nuclear localization [5].


  1. The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein. Canton, D.A., Olsten, M.E., Kim, K., Doherty-Kirby, A., Lajoie, G., Cooper, J.A., Litchfield, D.W. Mol. Cell. Biol. (2005) [Pubmed]
  2. CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM. Zhang, L., Tie, Y., Tian, C., Xing, G., Song, Y., Zhu, Y., Sun, Z., He, F. Cell. Signal. (2006) [Pubmed]
  3. Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosis. Zhang, L., Xing, G., Tie, Y., Tang, Y., Tian, C., Li, L., Sun, L., Wei, H., Zhu, Y., He, F. EMBO J. (2005) [Pubmed]
  4. The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling. Zhang, L., Tang, Y., Tie, Y., Tian, C., Wang, J., Dong, Y., Sun, Z., He, F. Cell. Signal. (2007) [Pubmed]
  5. Functional specialization of CK2 isoforms and characterization of isoform-specific binding partners. Litchfield, D.W., Bosc, D.G., Canton, D.A., Saulnier, R.B., Vilk, G., Zhang, C. Mol. Cell. Biochem. (2001) [Pubmed]
  6. The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane. Olsten, M.E., Canton, D.A., Zhang, C., Walton, P.A., Litchfield, D.W. J. Biol. Chem. (2004) [Pubmed]
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