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Gene Review

CKAP4  -  cytoskeleton-associated protein 4

Homo sapiens

Synonyms: 63-kDa cytoskeleton-linking membrane protein, CLIMP-63, Climp-63, Cytoskeleton-associated protein 4, ERGIC-63, ...
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Disease relevance of CKAP4


High impact information on CKAP4

  • Relationships between p63 binding, DNA sequence, transcription activity, and biological function in human cells [5].
  • There is a significant, but complex, relationship between p63 target sites and p63-responsive genes, with DeltaNp63 isoforms being linked to transcriptional activation [5].
  • Using tiled microarrays covering the entire human genome, we identify approximately 5800 target sites for p63, a p53 homolog essential for stratified epithelial development. p63 targets are enriched for genes involved in cell adhesion, proliferation, death, and signaling pathways [5].
  • The quality of the derived DNA sequence motif for p63 targets correlates with binding strength binding in vivo, but only a small minority of motifs in the genome is bound by p63 [5].
  • The tyrosine phosphorylation of p63 can be induced independently of other substrates when using a single CD2 mAb recognizing the D66 epitope of the molecule [6].

Chemical compound and disease context of CKAP4


Biological context of CKAP4

  • This study aims to verify the relationship between p63 expression and several clinicopathological features and tumor markers of clinical significance in breast pathology including key regulators of the cell cycle, oncogenes, apoptosis-related proteins, metalloproteinases and their inhibitors [1].
  • Mitotic phosphorylation can be prevented by mutation of serines 3, 17, and 19 in the cytoplasmic domain of CLIMP-63 [10].
  • Metabolic labeling with (32)P showed that CLIMP-63 is a phosphoprotein with increased phosphorylation during mitosis [10].
  • Overexpression of the phospho-mimicking mitotic form of CLIMP-63 in interphase cells leads to a collapse of the ER around the nucleus, leaving the microtubular network intact [10].
  • An additional remarkable feature of p63 is that it becomes reversibly palmitoylated when intracellular protein transport is blocked by the drug brefeldin A [11].

Anatomical context of CKAP4

  • Immunofluorescence microscopy demonstrated that p63 was located principally in the endoplasmic reticulum but was also detected in significant quantities on the surface of human VSMC [12].
  • p63, a p53 homologue, is a myoepithelial cell marker in the normal mammary gland but p63-positive neoplastic cells may be found in up to 11% of invasive breast carcinomas [1].
  • Concentration of CLIMP-63 into patches may enhance microtubule binding on the cytosolic side and contribute to ER morphology by the formation of a protein scaffold in the lumen of the ER [13].
  • The findings indicate that the luminal segment of CLIMP-63 is necessary and sufficient for oligomerization into alpha-helical complexes that prevent nuclear envelope localization [13].
  • Here we first characterize young primary NHP cells as CK5(+)/CK18(+) intermediate basal cells that also express several other putative stem/progenitor cell markers including p63, CD44, alpha2beta1, and hTERT [14].

Associations of CKAP4 with chemical compounds


Other interactions of CKAP4

  • The recently identified 63 kDa membrane protein, p63, is a resident protein of a membrane network interposed in between rough ER and Golgi apparatus [11].

Analytical, diagnostic and therapeutic context of CKAP4


  1. The differential regulation of human telomerase reverse transcriptase and vascular endothelial growth factor may contribute to the clinically more aggressive behavior of p63-positive breast carcinomas. Ribeiro-Silva, A., Becker de Moura, H., Ribeiro do Vale, F., Zucoloto, S. Int. J. Biol. Markers (2005) [Pubmed]
  2. The major surface protein of Leishmania promastigotes is anchored in the membrane by a myristic acid-labeled phospholipid. Etges, R., Bouvier, J., Bordier, C. EMBO J. (1986) [Pubmed]
  3. Homeobox gene Dlx3 is regulated by p63 during ectoderm development: relevance in the pathogenesis of ectodermal dysplasias. Radoja, N., Guerrini, L., Lo Iacono, N., Merlo, G.R., Costanzo, A., Weinberg, W.C., La Mantia, G., Calabr??, V., Morasso, M.I. Development (2007) [Pubmed]
  4. CKAP4/p63 Is a Receptor for the Frizzled-8 Protein-related Antiproliferative Factor from Interstitial Cystitis Patients. Conrads, T.P., Tocci, G.M., Hood, B.L., Zhang, C.O., Guo, L., Koch, K.R., Michejda, C.J., Veenstra, T.D., Keay, S.K. J. Biol. Chem. (2006) [Pubmed]
  5. Relationships between p63 binding, DNA sequence, transcription activity, and biological function in human cells. Yang, A., Zhu, Z., Kapranov, P., McKeon, F., Church, G.M., Gingeras, T.R., Struhl, K. Mol. Cell (2006) [Pubmed]
  6. Tyrosine phosphorylation and association with phospholipase C gamma-1 of the GAP-associated 62-kD protein after CD2 stimulation of Jurkat T cell. Hubert, P., Debré, P., Boumsell, L., Bismuth, G. J. Exp. Med. (1993) [Pubmed]
  7. Antibodies against a synthetic peptide of the poliovirus replicase protein: reaction with native, virus-encoded proteins and inhibition of virus-specific polymerase activities in vitro. Baron, M.H., Baltimore, D. J. Virol. (1982) [Pubmed]
  8. Distinction of pulmonary small cell carcinoma from poorly differentiated squamous cell carcinoma: an immunohistochemical approach. Zhang, H., Liu, J., Cagle, P.T., Allen, T.C., Laga, A.C., Zander, D.S. Mod. Pathol. (2005) [Pubmed]
  9. Gleevec suppresses p63 expression in head and neck squamous cell carcinoma despite p63 activation by DNA-damaging agents. Ongkeko, W.M., An, Y., Chu, T.S., Aguilera, J., Dang, C.L., Wang-Rodriguez, J. Laryngoscope (2006) [Pubmed]
  10. Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules. Vedrenne, C., Klopfenstein, D.R., Hauri, H.P. Mol. Biol. Cell (2005) [Pubmed]
  11. A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein. Schweizer, A., Rohrer, J., Jenö, P., DeMaio, A., Buchman, T.G., Hauri, H.P. J. Cell. Sci. (1993) [Pubmed]
  12. Functional regulation of tissue plasminogen activator on the surface of vascular smooth muscle cells by the type-II transmembrane protein p63 (CKAP4). Razzaq, T.M., Bass, R., Vines, D.J., Werner, F., Whawell, S.A., Ellis, V. J. Biol. Chem. (2003) [Pubmed]
  13. Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment. Klopfenstein, D.R., Klumperman, J., Lustig, A., Kammerer, R.A., Oorschot, V., Hauri, H.P. J. Cell Biol. (2001) [Pubmed]
  14. Cell-autonomous induction of functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) contributes to replicative senescence of human prostate progenitor cells. Bhatia, B., Tang, S., Yang, P., Doll, A., Aumüeller, G., Newman, R.A., Tang, D.G. Oncogene (2005) [Pubmed]
  15. p63 regulates an adhesion programme and cell survival in epithelial cells. Carroll, D.K., Carroll, J.S., Leong, C.O., Cheng, F., Brown, M., Mills, A.A., Brugge, J.S., Ellisen, L.W. Nat. Cell Biol. (2006) [Pubmed]
  16. Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers. Schweizer, A., Rohrer, J., Hauri, H.P., Kornfeld, S. J. Cell Biol. (1994) [Pubmed]
  17. A three-dimensional model of differentiation of immortalized human bronchial epithelial cells. Vaughan, M.B., Ramirez, R.D., Wright, W.E., Minna, J.D., Shay, J.W. Differentiation (2006) [Pubmed]
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