Disease relevance of ACBD3

• These studies showed that, like in the mouse, human PAP7 is highly expressed in steroidogenic tissues, where it follows the pattern of PRKAR1A expression, suggesting that it participates in PRKAR1A-mediated tumorigenesis and hypercortisolism [1].

High impact information on ACBD3

• We report that Dexras1 binds to the peripheral benzodiazepine receptor-associated protein (PAP7), a protein of unknown function that binds to cyclic AMP-dependent protein kinase and the peripheral benzodiazepine receptor [2].
• The Iip35 isoform of the major histocompatibility complex (MHC) class II-associated invariant chain (Ii) contains an endoplasmic reticulum (ER) targeting motif, but in B cell lines the ER retention is ineffective and a fraction of Iip35 is transported through the Golgi complex associated with class II molecules [3].
• Co-expression of Tspo, Pap7, PkarIalpha, and Star genes resulted in the stimulation of steroid formation in both steroidogenic MA-10 and non-steroidogenic COS-F2-130 cells that were engineered to metabolize cholesterol [4].
• We used a yeast two-hybrid assay to screen for interactors of the golgin-160 head and identified GCP60 (Golgi complex-associated protein of 60 kDa) [5].
• In addition, cells overexpressing GCP60 were more sensitive to apoptosis induced by staurosporine, suggesting that nuclear-localized golgin-160-(140-311) might promote cell survival [5].

Biological context of ACBD3

• Overexpression of the COOH-terminal domain of GCP60 caused disassembly of the Golgi structure and blocked protein transport from the endoplasmic reticulum to the Golgi [6].
• Treatment of MA-10 cells with oligonucleotides antisense to PAP7 also inhibited the hCG-stimulated steroid formation, suggesting that PAP7 is a functional element of the hormone-induced signal transduction cascade leading to steroidogenesis [7].
• The full-length mouse PAP7 gene was cloned and assembled by screening a BAC clone, polymerase chain reaction and searching the mouse genome database [8].
• Although it is shorter than the human PAP7 gene, all exons are conserved between the mouse and human [8].
• The mouse PAP7 gene was mapped to chromosome 1H3-5 by fluorescence in situ hybridization in agreement with in silico search of the mouse genome database that mapped the PAP7 cDNA sequence to the 1H4 area [8].

Anatomical context of ACBD3

• The 3.6-kilobase mRNA encoding a 528-amino acid protein of 60 kDa designated GCP60 was ubiquitously expressed and was especially abundant in the testis and ovary [6].
• Immunofluorescence and immunoelectron microscopy confirmed that GCP60 was co-localized with giantin in the Golgi complex [6].
• Hormone treatment of MA-10 Leydig cells induced the co-localization of TSPO, PAP7, PKARIalpha, and StAR in mitochondria, visualized by confocal microscopy, and the formation in living cells of a high molecular weight multimeric complex identified using photoactivable amino acids [4].
• Immunohistochemical and in situ hybridization studies indicated that PAP7 is highly expressed in the gonads, adrenal, hippocampus, and distinct brain neuronal and glial populations [7].
• Like PRKAR1A, PAP7 was decreased in CNC lymphocytes and PPNAD nodules, but not in the surrounding cortex [1].

Associations of ACBD3 with chemical compounds

• Overexpression of the full length PAP7 increased the hCG-induced steroid production [7].
• The predicted protein, GCP364 (for a Golgi complex-associated protein of 364 kDa), was found to have no NH2-terminal signal sequence but a single hydrophobic domain at the COOH terminus and characteristically contain many coiled-coil domains with various sizes throughout the entire sequence [9].

Physical interactions of ACBD3

• Taken together, these results suggest that GCP60 is involved in the maintenance of the Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and the Golgi [6].

Other interactions of ACBD3

• PAP7 and PRKAR1A expression were studied in PPNAD and in lymphoblasts from patients bearing PRKAR1A-mut [1].
• Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin [6].
• Golgi phosphoprotein of 130 kDa (GPP130) is a cis-Golgi protein that allows assay of retrieval-based targeting because it redistributes to endosomes upon treatment with agents that disrupt lumenal pH, and it undergoes endosome-to-Golgi retrieval upon drug removal [10].
• This strong interaction prevented the golgin-160 fragment from accumulating in the nucleus when this fragment and GCP60 were overexpressed [5].

References