Disease relevance of CENTB1

• In addition, CENTB1 mRNA level is increased in the inflamed mucosa of patients with inflammatory bowel disease [1].

High impact information on CENTB1

• ACAP1 and ACAP2 are widely expressed and occur together in the various cultured cell lines we examined [2].
• In HeLa cells, overexpression of either ACAP blocked the formation of Arf6-dependent protrusions [2].
• We also demonstrate that endogenous CENTB1 interacts with endogenous NOD2 and NOD1 in SW480 and HT-29 intestinal epithelial cells [1].
• Centaurin beta1 (CENTB1), a GTPase-activating protein, is a member of the ADP-ribosylation factor family encoded by a gene located on the short arm of human chromosome 17 [1].
• Remarkably, all of these phenotypes, including accumulated tubular endosomes, blocked recycling, and failure to make protrusions and recruit ACAP effectively, could be recreated in either untransfected cells or cells expressing wild-type Arf6 by treatment with 1-butanol to inhibit the formation of phosphatidic acid (PA), the product of PLD [3].

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].

References