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ADAP1  -  ArfGAP with dual PH domains 1

Homo sapiens

Synonyms: Arf-GAP with dual PH domain-containing protein 1, CENTA1, Centaurin-alpha-1, Cnt-a1, GCS1L, ...
 
 
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Disease relevance of CENTA1

 

Psychiatry related information on CENTA1

 

High impact information on CENTA1

 

Biological context of CENTA1

  • Centaurin-alpha is a 46 kDa in vitro binding protein for the lipid second messenger PtdIns(3,4,5)P3 [6].
  • Here, elucidating the gene structure for both proteins, we found the human gene for centaurin alpha2 located on chromosome 17, position 17q11.2, near to the NF1 locus, and human p42IP4 on chromosome 7, position 7p22 [1].
  • A deletion mutant of p42IP4 lacking the zinc finger domain resulted in solely a cytosolic and membrane localization but was not found in the nucleus [7].
  • The cDNA sequence of the human p42IP4 containing a single open reading frame yields a peptide of 374 amino acids with a calculated molecular mass of 43.4 kDa with a zinc-finger motif at the N-terminus, followed by two pleckstrin homology (PH) domains [7].
  • CENTA is a newly synthesized, beta-lactamase-labile, chromogenic cephalosporin reagent which changes color from light yellow (lambda maximum ca. 340 nm) to chrome yellow (lambda maximum ca. 405 nm) concomitant with hydrolysis of the beta-lactam ring [8].
 

Anatomical context of CENTA1

 

Associations of CENTA1 with chemical compounds

  • Furthermore, fusion proteins of centaurin alpha2 and p42IP4, respectively, with the green fluorescent protein (GFP) were expressed in HEK 293 cells to visualize subcellular distribution [1].
  • In this study we describe for the human inositol-(1,3,4,5)-tetrakisphosphate (InsP4)-binding protein, p42IP4, the cellular distribution and subcellular localization in human brain and in transfected neuronal cells [7].
 

Other interactions of CENTA1

 

Analytical, diagnostic and therapeutic context of CENTA1

References

  1. Identification of gene structure and subcellular localization of human centaurin alpha 2, and p42IP4, a family of two highly homologous, Ins 1,3,4,5-P4-/PtdIns 3,4,5-P3-binding, adapter proteins. Hanck, T., Stricker, R., Sedehizade, F., Reiser, G. J. Neurochem. (2004) [Pubmed]
  2. Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin alpha. Reiser, G., Bernstein, H.G. Neuroreport (2002) [Pubmed]
  3. Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteins. Dubois, T., Kerai, P., Zemlickova, E., Howell, S., Jackson, T.R., Venkateswarlu, K., Cullen, P.J., Theibert, A.B., Larose, L., Roach, P.J., Aitken, A. J. Biol. Chem. (2001) [Pubmed]
  4. Identification and cloning of centaurin-alpha. A novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brain. Hammonds-Odie, L.P., Jackson, T.R., Profit, A.A., Blader, I.J., Turck, C.W., Prestwich, G.D., Theibert, A.B. J. Biol. Chem. (1996) [Pubmed]
  5. Centaurin-alpha 1, an ADP-ribosylation factor 6 GTPase activating protein, inhibits beta 2-adrenoceptor internalization. Lawrence, J., Mundell, S.J., Yun, H., Kelly, E., Venkateswarlu, K. Mol. Pharmacol. (2005) [Pubmed]
  6. Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Venkateswarlu, K., Oatey, P.B., Tavaré, J.M., Jackson, T.R., Cullen, P.J. Biochem. J. (1999) [Pubmed]
  7. Cellular expression and subcellular localization of the human Ins(1,3,4,5)P(4)-binding protein, p42(IP4), in human brain and in neuronal cells. Sedehizade, F., Hanck, T., Stricker, R., Horstmayer, A., Bernstein, H.G., Reiser, G. Brain Res. Mol. Brain Res. (2002) [Pubmed]
  8. In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagent. Jones, R.N., Wilson, H.W., Novick, W.J., Barry, A.L., Thornsberry, C. J. Clin. Microbiol. (1982) [Pubmed]
  9. The arf6 GAP centaurin alpha-1 is a neuronal actin-binding protein which also functions via GAP-independent activity to regulate the actin cytoskeleton. Thacker, E., Kearns, B., Chapman, C., Hammond, J., Howell, A., Theibert, A. Eur. J. Cell Biol. (2004) [Pubmed]
  10. Centaurin-alpha 1 associates in vitro and in vivo with nucleolin. Dubois, T., Zemlickova, E., Howell, S., Aitken, A. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  11. Molecular cloning and functional characterization of a human homologue of centaurin-alpha. Venkateswarlu, K., Cullen, P.J. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  12. Interaction of the brain-specific protein p42IP4/centaurin-alpha1 with the peptidase nardilysin is regulated by the cognate ligands of p42IP4, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4, with stereospecificity. Stricker, R., Chow, K.M., Walther, D., Hanck, T., Hersh, L.B., Reiser, G. J. Neurochem. (2006) [Pubmed]
 
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