AI Article Synopsis
- KLHY is a short, conserved amino-acid sequence in inhibitor-2 that relates to the binding of protein phosphatase 1 (PP1), but its specific role in binding is unclear.
- Research utilizing surface plasmon resonance indicated that altering or removing KLHY did not significantly change the binding strength between inhibitor-2 and PP1.
- In contrast to DARPP-32, where removing its PP1-binding motif drastically reduced affinity, the KLHY sequence in inhibitor-2 showed weaker binding to PP1 overall.
Article Abstract
KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.
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| http://dx.doi.org/10.1093/jb/mvi167 | DOI Listing |
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