Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's Disease
Article first published online: 21 JAN 2003
Copyright © 2003 Wiley Periodicals, Inc.
Volume 25, Issue 2, pages 174–181, February 2003
How to Cite
Lu, K. P., Liou, Y.-C. and Vincent, I. (2003), Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's Disease. Bioessays, 25: 174–181. doi: 10.1002/bies.10223
- Issue published online: 21 JAN 2003
- Article first published online: 21 JAN 2003
- NIH (grants GM56230, GM58556 and AG17870 to K.P.L., AG12721 to I. V., P50 AG05136-16) (Murray Raskind, PI)
- the Alzheimer Association (IIRG-99-18)
- the American Health Assistance Fund (1999039) to I.V
The reversible phosphorylation of proteins on serine/threonine residues preceding proline (Ser/Thr-Pro) is a major regulatory mechanism for the control of a series of cell cycle events. Although phosphorylation is thought to regulate protein function by inducing conformational changes, little is known about most of these conformational changes and their significance. Recent studies indicate that the conformation and function of a subset of these phosphorylated proteins are controlled by the prolyl isomerase Pin1 through isomerization of specific phosphorylated Ser/Thr-Pro bonds. Furthermore, compelling evidence supports the idea that proline-directed phosphorylation and subsequent isomerization play a critical role not only in cell cycle control, but also in the development of Alzheimer's disease, where postmitotic neurons display various cell cycle markers, especially mitotic events, prior to degeneration. BioEssays 25:174–181, 2003. © 2003 Wiley Periodicals, Inc.