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Gene Review

ACAP1  -  ArfGAP with coiled-coil, ankyrin repeat...

Homo sapiens

Synonyms: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1, CENTB1, Centaurin-beta-1, Cnt-b1, KIAA0050
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Disease relevance of CENTB1


High impact information on CENTB1


Biological context of CENTB1

  • Disrupting the activities of either ACAP1 or Akt, or their assembly with endosomal beta1, inhibits beta1 recycling and cell migration [4].
  • However, in contrast to TfR recycling, the role of ACAP1 in beta1 recycling requires its phosphorylation by Akt, which is, in turn, regulated by a canonical signaling pathway [4].
  • Truncated and point mutations in the ACAP1 BAR and PH domains revealed that both BAR and PH domains are required for tubulation [5].

Anatomical context of CENTB1

  • In addition, ACAP1 and ACAP2 were recruited to peripheral, tubular membranes, where activation of Arf6 occurs to allow membrane recycling back to the plasma membrane [2].
  • Moreover, ACAP1 binds to two distinct phenylalanine-based sequences in the cytoplasmic domain of TfR that function as recycling sorting signals to promote its transport from the recycling endosome [6].

Associations of CENTB1 with chemical compounds

  • CENTB1 expression in epithelial cells was highly induced by tumor necrosis factor alpha, interleukin 1beta, and the NOD1 and NOD2 ligands (gamma-d-glutamyl-meso-diaminopimelic acid and muramyl dipeptide, respectively) [1].
  • We now show that ACAP1 also participates in the regulated recycling of integrin beta1 to control cell migration [4].
  • ACAP1 has a pleckstrin homology (PH) domain known to bind phosphoinositide and a Bin/amphiphysin/Rvs (BAR) domain that has been reported to detect membrane curvature [5].
  • The latency of waves I, III, V and ACAP (Auditory Compound Action Potential) and intervals between waves I-III, III-V, I-V and ACAP-V were analysed as functions of stimulus intensity in pre- and post-exposure recordings [7].

Co-localisations of CENTB1

  • CENTB1 partially co-localized with NOD2 and NOD1 proteins in the cytoplasm of mammalian cells [1].

Other interactions of CENTB1

  • While there were few tubules induced by the expression of ACAP1 alone, numerous endosomal tubules were induced by coexpression of PIP5K and ACAP1 [5].

Analytical, diagnostic and therapeutic context of CENTB1

  • Normal breast acini were patchily reactive for ACAP-1, whereas CaMp and ACC-1 stainings were more diffuse [8].


  1. Centaurin beta1 Down-regulates Nucleotide-binding Oligomerization Domains 1- and 2-dependent NF-{kappa}B Activation. Yamamoto-Furusho, J.K., Barnich, N., Xavier, R., Hisamatsu, T., Podolsky, D.K. J. Biol. Chem. (2006) [Pubmed]
  2. ACAPs are arf6 GTPase-activating proteins that function in the cell periphery. Jackson, T.R., Brown, F.D., Nie, Z., Miura, K., Foroni, L., Sun, J., Hsu, V.W., Donaldson, J.G., Randazzo, P.A. J. Cell Biol. (2000) [Pubmed]
  3. An effector domain mutant of Arf6 implicates phospholipase D in endosomal membrane recycling. Jovanovic, O.A., Brown, F.D., Donaldson, J.G. Mol. Biol. Cell (2006) [Pubmed]
  4. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration. Li, J., Ballif, B.A., Powelka, A.M., Dai, J., Gygi, S.P., Hsu, V.W. Dev. Cell (2005) [Pubmed]
  5. Cooperation of Phosphoinositides and BAR Domain Proteins in Endosomal Tubulation. Shinozaki-Narikawa, N., Kodama, T., Shibasaki, Y. Traffic (2006) [Pubmed]
  6. ACAP1 promotes endocytic recycling by recognizing recycling sorting signals. Dai, J., Li, J., Bos, E., Porcionatto, M., Premont, R.T., Bourgoin, S., Peters, P.J., Hsu, V.W. Dev. Cell (2004) [Pubmed]
  7. Studies on the temporary effect of noise on the auditory function in man. Fiałkowska, M.D., Janczewski, G., Kochanek, K., Dawidowicz, J. Scandinavian audiology. (1983) [Pubmed]
  8. Immunocytochemical demonstration of calmodulin and its activated forms in normal and carcinomatous human mammary tissue. Tuccari, G., Rizzo, A., Barresi, G. European journal of histochemistry : EJH. (1993) [Pubmed]
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