Research Project
Grant-in-Aid for Young Scientists (B)
Voltage-sensing phosphatase, VSP, has an activity to dephosphorylate several kinds of phosphoinositides in a voltage-dependent manner. Our recent study has shown that VSP mainly dephosphoryltaes PI(3,4,5)P3 in low membrane voltages but dephosphorylates PI(3,4)P2 in high voltages. However, little is know about the molecular mechanisms how the membrane voltage regulates the substrate specificity of VSP. In this work, I introduced a fluorescent label using the method of the genetic incorporation of a fluorescent unnatural amino acid to reveal the conformational change of the catalytic region which is responsible for the dephosphorylation activity. Results showed that Cα2 loop located in the catalytic region plays key roles in the substrate specificity in VSP.
All 2016 2015 2014 2013 Other
All Journal Article (6 results) (of which Peer Reviewed: 6 results, Open Access: 5 results, Acknowledgement Compliant: 1 results) Presentation (4 results) Remarks (1 results)
Annu Rev Biochem.
Volume: 84 Issue: 1 Pages: 685-709
10.1146/annurev-biochem-060614-034307
Physiological Reports
Volume: 2 Issue: 7 Pages: 1-13
10.14814/phy2.12061
J. Physiol.
Volume: 592(Pt 5) Issue: 5 Pages: 899-914
10.1113/jphysiol.2013.263640
Neurology
Volume: 82 Issue: 12 Pages: 1058-64
10.1212/wnl.0000000000000239
Nat. Strucl. & Mol. Biol.
Volume: (4) Issue: 4 Pages: 352-7
10.1038/nsmb.2783
J. Cell Physiol.
Volume: 229(4) Issue: 4 Pages: 422-33
10.1002/jcp.24463
http://www.med.osaka-u.ac.jp/pub/phys2/okamura/