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Proline‐directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's Disease
Author(s) -
Lu Kun Ping,
Liou YihCherng,
Vincent Inez
Publication year - 2003
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.10223
Subject(s) - pin1 , phosphorylation , prolyl isomerase , threonine , serine , proline , mitosis , microbiology and biotechnology , cell cycle , cis trans isomerases , biology , biochemistry , function (biology) , peptidylprolyl isomerase , protein phosphorylation , isomerase , chemistry , cell , protein kinase a , enzyme , amino acid
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.