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The phosphorylation of specific proteins on Ser/Thr residues preceding proline is thought to be a major cellular signaling mechanism; however, very little is known about how the phosphorylation actually regulates protein function. Pin1 is an 18 kDa protein with two domains: the N-terminal WW domain (named after two invariant Trp residues, amino acids 1-39) and the C-terminal PPIase domain (amino acids 45-163). The WW domain acts as a binding module to bind its substrate via the phosphoserine (p-Ser) or phosphothreonine (p-Thr)-proline motifs in its substrates. The C-terminal PPIase domain is the catalytic domain to isomerize the conformational changes of specific pSer/Thr-Pro motifs. Unlike other peptidyl-prolyl isomerases (PPIases), Pin1 is a unique peptidyl isomerase that recognizes only the phosphorylated Ser/Thr motif preceding a proline residue. In addition, Pin1 is very prominent in isomerizing the cis-trans conformation of prolyl-peptidyl bonds in its substrates, resulting in regulation of their biological functions, suggesting the conformational changes mediated by Pin1 or Pin1-like isomerase may be crucial for the normal functioning of cells.
The phosphorylation of specific proteins on Ser/Thr residues preceding proline is thought to be a major cellular signaling mechanism; however, very little is known about how the phosphorylation actually regulates protein function. Pin1 is an 18 kDa protein with two domains: the N-terminal WW domain (named after two invariant Trp residues, amino acids 1-39) and the C-terminal PPIase domain (amino acids 45-163). The WW domain acts as a binding module to bind its substrate via the phosphoserine (p-Ser) or phosphothreonine (p-Thr)-proline motifs in its substrates. The C-terminal PPIase domain is the catalytic domain to isomerize the conformational changes of specific pSer/Thr-Pro motifs. Unlike other peptidyl-prolyl isomerases (PPIases), Pin1 is a unique peptidyl isomerase that recognizes only the phosphorylated Ser/Thr motif preceding a proline residue. In addition, Pin1 is very prominent in isomerizing the cis-trans conformation of prolyl-peptidyl bonds in its substrates, resulting in regulation of their biological functions, suggesting the conformational changes mediated by Pin1 or Pin1-like isomerase may be crucial for the normal functioning of cells.
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ADVANCED SCIENCEno. 3 (2024)
Bone Researchno. 1 (2024): 1-30
Ming Chen,Kaili Cen,Yinjing Song,Xiaochen Zhang,Yih-Cherng Liou,Pu Liu, Jinyan Huang,Jian Ruan, Jia He, Wanyi Ye,Tianyue Wang,Xing Huang,
Cancer letters (2023): 216285-216285
Hong Zheng,Minghao Wang,Shiyu Zhang,Dongxue Hu,Qiaoyun Yang,Ming Chen, Xia Zhang,Yi Zhang,Jigang Dai,Yih-Cherng Liou
International journal of biological sciencesno. 14 (2023): 4689-4708
Darren Chen Pei Wong,Zekun Xia,Nandi Shao, Jin Ye Yeo,Ivan Yow, T. Thivakar,Andres M. Salazar,Yih-Cherng Liou,Boon Chuan Low,Jeak Ling Ding
biorxiv(2023)
crossref(2023)
Frontiers in Cell and Developmental Biology (2023): 1225128
Advanced science (Weinheim, Baden-Wurttemberg, Germany)no. 3 (2023): e2306535-e2306535
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