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Gene Review

AJUBA  -  ajuba LIM protein

Homo sapiens

Synonyms: JUB, LIM domain-containing protein ajuba, MGC15563
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High impact information on JUB

  • In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A [1].
  • A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein [1].
  • We show that cells from Ajuba null mice are inhibited in their migration, without associated abnormality in adhesion to extracellular matrix proteins, cell spreading, or integrin activation [2].
  • In migrating primary mouse embryonic fibroblasts (MEFs) from Ajuba(-/-) mice the level of PI(4,5)P2 was decreased with a corresponding increase in the level of the substrate PI(4)P [3].
  • The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha [3].

Biological context of JUB

  • Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry [1].
  • Thus, in addition to its effects upon Rac activity Ajuba can also influence cell migration through regulation of PI(4,5)P2 synthesis through direct activation of PIPKIalpha enzyme activity [3].
  • To understand Ajuba's role in signal transduction pathways, we performed a yeast two-hybrid screen with the LIM domain region of Ajuba [4].
  • The Zyxin/Ajuba family of cytosolic LIM domain-containing proteins has the potential to shuttle from sites of cell adhesion into the nucleus and thus can be candidate transducers of environmental signals [4].
  • Here we show that, in primary keratinocytes, the LIM domain protein Ajuba is recruited to cadherin-dependent cell-cell adhesive complexes in a regulated manner [5].

Anatomical context of JUB

  • Localization of PI(4,5)P2 synthesis and PIPKIalpha in the leading lamellipodia and membrane ruffles, respectively, of migrating Ajuba(-/-) MEFs was impaired [3].
  • Keratinocytes from Ajuba null mice exhibit abnormal cell-cell junction formation and/or stability and function [5].
  • At cadherin adhesive complexes Ajuba interacts with alpha-catenin, and alpha-catenin is required for efficient recruitment of Ajuba to cell junctions [5].
  • Ajuba is expressed in cerebellum, cortex, hippocampus, and retina and also in organs outside the CNS [6].

Physical interactions of JUB

  • Ajuba LIM domains directly bind to Gfi1, but the association is not SNAG domain-dependent [7].

Other interactions of JUB


  1. Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Hirota, T., Kunitoku, N., Sasayama, T., Marumoto, T., Zhang, D., Nitta, M., Hatakeyama, K., Saya, H. Cell (2003) [Pubmed]
  2. The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration. Pratt, S.J., Epple, H., Ward, M., Feng, Y., Braga, V.M., Longmore, G.D. J. Cell Biol. (2005) [Pubmed]
  3. The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha. Kisseleva, M., Feng, Y., Ward, M., Song, C., Anderson, R.A., Longmore, G.D. Mol. Cell. Biol. (2005) [Pubmed]
  4. The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex. Feng, Y., Longmore, G.D. Mol. Cell. Biol. (2005) [Pubmed]
  5. The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin. Marie, H., Pratt, S.J., Betson, M., Epple, H., Kittler, J.T., Meek, L., Moss, S.J., Troyanovsky, S., Attwell, D., Longmore, G.D., Braga, V.M. J. Biol. Chem. (2003) [Pubmed]
  6. The amino terminus of the glial glutamate transporter GLT-1 interacts with the LIM protein Ajuba. Marie, H., Billups, D., Bedford, F.K., Dumoulin, A., Goyal, R.K., Longmore, G.D., Moss, S.J., Attwell, D. Mol. Cell. Neurosci. (2002) [Pubmed]
  7. Ajuba functions as a histone deacetylase-dependent co-repressor for autoregulation of the growth factor-independent-1 transcription factor. Montoya-Durango, D.E., Velu, C.S., Kazanjian, A., Rojas, M.E., Jay, C.M., Longmore, G.D., Grimes, H.L. J. Biol. Chem. (2008) [Pubmed]
  8. LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis. Abe, Y., Ohsugi, M., Haraguchi, K., Fujimoto, J., Yamamoto, T. FEBS Lett. (2006) [Pubmed]
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