| First Author | Bennett D | Year | 1999 |
| Journal | Biochemistry | Volume | 38 |
| Issue | 49 | Pages | 16276-82 |
| PubMed ID | 10587451 | Mgi Jnum | J:58884 |
| Mgi Id | MGI:1350540 | Doi | 10.1021/bi9917028 |
| Citation | Bennett D, et al. (1999) The chaperone-like properties of mammalian inhibitor-2 are conserved in a Drosophila homologue. Biochemistry 38(49):16276-82 |
| abstractText | Phosphatase inhibitor-2 (I-2) is a mammalian phosphoprotein that binds to the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1c) and inhibits its activity in vitro. Recombinant PP1c differs from native PP1c in several biochemical criteria, including the requirement for Mn(2+), sensitivity to vanadate, and p-nitrophenyl phosphate (pNPP) phosphatase activity. I-2 can convert recombinant PP1c into a native-like activity in vitro. It has therefore been suggested that I-2 may act as a molecular chaperone for PP1 in vivo. We have identified a Drosophila homologue (I-2Dm) in a two-hybrid screen for PP1c-binding proteins. The sequence of I-2Dm is 35% identical with that of I-2, whereas the catalytic subunits themselves are >85% identical in flies and humans; however, we show that many biochemical properties of I-2 are conserved. Like I-2, I-2Dm can convert recombinant PP1c to a native-like activity. This strongly suggests that this ability is an essential, conserved role of I-2 and I-2Dm. |
