Pinning down cell signaling, cancer and Alzheimer's disease

被引：219

作者：

Lu, KP ^{[1
]}

机构：

[1] Harvard Univ, Beth Israel Deaconess Med Ctr, Sch Med, Dept Med,Div Hematol Oncol,Canc Biol Program, Boston, MA 02215 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2004年 / 29卷 / 04期

关键词：

D O I：

10.1016/j.tibs.2004.02.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein phosphorylation on certain serine or threonine residues preceding proline (Ser/Thr-Pro) is a pivitol signaling mechanism in diverse cellular processes and its deregulation can lead to human disease. However, little is known about how these phosphorylation events actually control cell signaling. Pin1 is a highly conserved enzyme that isomerizes only the phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Recent results indicate that such conformational changes following phosphorylation are a novel signaling mechanism pivotal in regulating many cellular functions. This mechanism also offers new insights into the pathogenesis and treatment of human disease, most notably cancer and Alzheimer's disease. Thus, Pin1 plays a key role in linking signal transduction to the pathogenesis of cancer and Alzheimer's disease - two major age-related diseases.

引用

页码：200 / 209

页数：10

共 75 条

[1] Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments [J].