Disease relevance of YIP3

• Thus, PRA1 associates with envelope glycoproteins from widely divergent lentiviruses [1].
• Interestingly, PRA1 also interacted with the Env CDs of HIV-2, bovine immunodeficiency virus, equine infectious anemia virus, and feline immunodeficiency virus [1].
• Although the human immunodeficiency virus (HIV-1) gp41 CD failed to interact with PRA1 in the yeast two-hybrid system, its interaction with PRA1 was significantly better than that of the SIV gp41 CD in mammalian two-hybrid assays [1].
• However, variation in the levels of PRA1 expression did not influence virion production, infectivity or envelope incorporation under the conditions of these assays [2].
• PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation [2].

High impact information on YIP3

• Replacement of the deleted VAMP2 transmembrane domain by a CAAX prenylation signal can not restore binding to PRA1 [3].
• PRA1 is a 21-kDa protein associated with Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state [1].
• Furthermore, gp41 sequences important for PRA1 binding were mapped to a central leucine-rich, amphipathic alpha-helix in the SIV gp41 cytoplasmic tail [1].
• Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor [1].
• The assembly and release of infectious virus particles was studied under conditions of PRA1 overexpression in a transient transfection assay or suppression by RNA interference [2].

Biological context of YIP3

• Vertical streak patterns of Pra1p and Phr1p indicated that post-translational modifications seem to be caused by variable glycosylation [4].
• By using a computational biology approach, we identified 180 potential cell-surface proteins in Candida albicans, including the known cell-surface adhesin Als1 and other cell-surface antigens, such as Pra1 and Csa1 [5].

Anatomical context of YIP3

• These data indicate that Yip3p may have multiple functions and that its interaction with Rabs is not critical for their recruitment to organelle membranes [6].

Physical interactions of YIP3

• We show here that the yeast (Saccharomyces cerevisiae) Golgi Rab GTPase Ypt1p can be copurified with the integral membrane protein Yip3p from detergent cell extracts [6].

Other interactions of YIP3

• However, Ypt1p did not copurify with Rtn1p, indicating that Yip3p is a component of at least two different protein complexes [6].

Analytical, diagnostic and therapeutic context of YIP3

• Mammalian two-hybrid assays confirmed the interaction between the SIV gp41 CD and PRA1 [1].

References