High impact information on PHO86

• Moreover, Pho84p is localized to the endoplasmic reticulum (ER) and fails to be targeted to the plasma membrane in the absence of Pho86p [1].
• The other three genes, GTR1, PHO86 and PHO87, are also suggested to be involved in the P(i) uptake system [2].
• PHO86 has two putative binding sites for the transcriptional activator, Pho4p, at nucleotide positions -191 and -497 relative to the ATG start codon, and showed substantial levels of transcription under high-P(i) conditions and more enhanced levels in low-P(i) medium [2].
• Both disruption and high dosage of PHO88 or PHO86 resulted in reduced Pi uptake [3].
• Increased dosage of PHO86, a gene encoding a putative membrane protein associated with a Pi transporter complex, activates the Pi-inhibited Pho81p produced under the control of the GAL1 promoter [3].

Biological context of PHO86

• The constitutive rAPase+ phenotype of the pho86 pho87 mutant was partially suppressed by an increased dosage of the PHO84 gene [4].

Anatomical context of PHO86

• Pho86p, an endoplasmic reticulum (ER) resident protein in Saccharomyces cerevisiae, is required for ER exit of the high-affinity phosphate transporter Pho84p [1].

Associations of PHO86 with chemical compounds

• Deletion of PHO86 in an ino1Delta strain resulted in faster growth when either phosphatidylinositol or glycerophosphoinositol was supplied as the sole inositol source [5].
• The delta pho86 delta pho88 double disruption resulted in enhanced synthesis of rAPase under the high-Pi condition and conferred arsenate resistance on the cells than those in single disruptants of these genes [3].
• A genetic screen identified Pho86p, which is required for targeting of the major phosphate transporter (Pho84p) to the plasma membrane, as affecting the utilization of phosphatidylinositol and glycerophosphoinositol [5].

Other interactions of PHO86

• This mutant has double mutations designated as pho86 and pho87 [4].
• These and the other findings suggest that the Pho86p and Pho87p proteins collaborate with Pho84p in Pi uptake [4].

Analytical, diagnostic and therapeutic context of PHO86

• Western blotting analysis of cell extracts revealed that Pho86p, tagged with c-Myc, was fractionated into a water-insoluble fraction [2].

References