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Gene Review

WWC1  -  WW and C2 domain containing 1

Homo sapiens

Synonyms: HBEBP3, HBEBP36, HBeAg-binding protein 3, KIAA0869, KIBRA, ...
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Disease relevance of WWC1

  • Finally we found that KIBRA interacts with histone H3 via its glutamic acid-rich region and that such interaction might play a mechanistic role in conferring an optimal ER transactivation function as well as the proliferation of ligand-stimulated breast cancer cells [1].

High impact information on WWC1

  • We found that KIBRA-DLC1 complex is recruited to ER-responsive promoters [1].
  • Our studies presented here revealed that KIBRA is a novel substrate for PKCzeta and suggest that PKCzeta phosphorylation may regulate the cellular function of KIBRA [2].
  • In a yeast two hybrid screen with the human isoform of Dendrin (KIAA0749), a putative modulator of the postsynaptic cytoskeleton, we isolated a cDNA coding for a novel protein, KIBRA, possessing two amino-terminal WW domains, an internal C2-like domain and a carboxy-terminal glutamic acid-rich stretch [3].
  • Characterization of KIBRA, a novel WW domain-containing protein [3].
  • Transient transfection of monkey kidney cells with constructs encoding Myc-tagged KIBRA displayed a cytoplasmic localization and a perinuclear enrichment of the protein [3].

Biological context of WWC1

  • A genomic locus encoding the brain protein KIBRA was significantly associated with memory performance in three independent, cognitively normal cohorts from Switzerland and the United States. Gene expression studies showed that KIBRA was expressed in memory-related brain structures [4].

Psychiatry related information on WWC1

  • We concluded that the KIBRA T-->C polymorphism contributes to modulate episodic memory amongst community-dwelling older adults free of dementia, but plays no obvious role in the phenotypic expression of MCI [5].

Associations of WWC1 with chemical compounds


Analytical, diagnostic and therapeutic context of WWC1

  • Northern blot analysis revealed that the expression of KIBRA mRNA was predominately found in kidney and brain [3].
  • We recently identified the neuronal protein KIBRA as novel member of this family of signal transducers [2].


  1. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. Rayala, S.K., den Hollander, P., Manavathi, B., Talukder, A.H., Song, C., Peng, S., Barnekow, A., Kremerskothen, J., Kumar, R. J. Biol. Chem. (2006) [Pubmed]
  2. KIBRA is a novel substrate for protein kinase Czeta. Büther, K., Plaas, C., Barnekow, A., Kremerskothen, J. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  3. Characterization of KIBRA, a novel WW domain-containing protein. Kremerskothen, J., Plaas, C., Büther, K., Finger, I., Veltel, S., Matanis, T., Liedtke, T., Barnekow, A. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  4. Common kibra alleles are associated with human memory performance. Papassotiropoulos, A., Stephan, D.A., Huentelman, M.J., Hoerndli, F.J., Craig, D.W., Pearson, J.V., Huynh, K.D., Brunner, F., Corneveaux, J., Osborne, D., Wollmer, M.A., Aerni, A., Coluccia, D., H??nggi, J., Mondadori, C.R., Buchmann, A., Reiman, E.M., Caselli, R.J., Henke, K., de Quervain, D.J. Science (2006) [Pubmed]
  5. KIBRA genetic polymorphism influences episodic memory in later life, but does not increase the risk of mild cognitive impairment. Almeida, O.P., Schwab, S.G., Lautenschlager, N.T., Morar, B., Greenop, K.R., Flicker, L., Wildenauer, D. J. Cell. Mol. Med. (2008) [Pubmed]
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