Disease relevance of RABAC1

• PRA1 promotes the intracellular trafficking and NF-kappaB signaling of EBV latent membrane protein 1 [1].
• The PRA1 protein was homologous to surface antigens of Aspergillus spp. which react with serum from aspergillosis patients, suggesting that the PRA1 protein may have a role in the host-parasite interaction during candidal infection [2].

High impact information on RABAC1

• Thus, PRA1 is required for vesicle formation from the Golgi complex and might be involved in recruitment of Rab effectors and SNARE proteins during cargo sequestration [3].
• The two PRA isoforms showed distinct intracellular localization with PRA1 localized primarily to the Golgi complex and PRA2 to the endoplasmic reticulum (ER) compartment [4].
• PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1 [5].
• The membrane-bound form can be partially extracted with physiological buffer and urea, suggesting that PRA1 is an extrinsic membrane protein [5].
• However, subcellular fractionation and immunocytochemical analyses indicated that PRA1 is localized both in the cytosol and tightly associated with the membrane compartment [5].

Biological context of RABAC1

• In addition, we have assigned the human PRA1 gene to chromosome 19q13.13-q13.2 and the human RILP gene to chromosome 17p13.3 [6].
• In contrast, PRAF1 may inhibit the herpes virus life cycle [7].
• Isolation and characterization of PRA1, a trypsin-like protease from the biocontrol agent Trichoderma harzianum CECT 2413 displaying nematicidal activity [8].

Anatomical context of RABAC1

• Here we show that the integral membrane protein, Yip3, acts catalytically to dissociate complexes of endosomal Rabs bound to GDI, and to deliver them onto membranes [9].
• Prenylated Rab acceptor domain family member 1 (PRAF1), a transmembrane protein whose precise function is unknown, localizes to the Golgi complex, post-Golgi vesicles, lipid rafts, endosomes, and the plasma membrane [7].
• Pursuing with the characterization of the biochemical interaction, we performed co-transfection experiments in COS-7 cells and we observed, by measurement of the intracellular cAMP produced and by FACS experiments, that the co-expression of two membrane proteins (PRA1, NIS, LH/CGR with TSHR) alters their expression [10].
• Several proteins with proteolytic activity were detected in culture filtrates from T. harzianum CECT 2413 grown in fungal cell walls or chitin and the protein responsible for the main activity (PRA1) was purified to homogeneity [8].

Associations of RABAC1 with chemical compounds

• In both H and N furosemide caused a significant rise of PRA1 (p less than 0.001 in H and p less than 0.01 in N) and PRA2 (p less than 0.001 in H and p less than 0.05 in N) [11].

Physical interactions of RABAC1

• It has been shown that PRA1 interacts with Rab proteins and with VAMP2 [6].

Other interactions of RABAC1

• The 0.8-kb mRNA for human PRA1 is ubiquitously expressed, while the two mRNAs for RILP are differentially expressed [6].
• Replication in a separate sample, consisting of 190 triplets, confirmed the exploratory data for the SCN8A (P = 0.005) and VAMP4 (P = 0.019) genes, but failed to confirm the data for the RABAC1 gene [12].

References