Peptidyl-prolyl isomerases: A new twist to transcription

EMBO Reports

Volumn 3, Issue 6, 2002, Pages 521-526

  Shaw, Pete E ^a  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; PARVULIN; POLYPEPTIDE; PROLINE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; NIMA INTERACTING PEPTIDYLPROLYL ISOMERASE; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE; RNA POLYMERASE II;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CATALYSIS; CELL CYCLE; CIS TRANS ISOMERISM; CONTROLLED STUDY; EUKARYOTIC CELL; IMMUNE SYSTEM; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; PROTEIN TARGETING; TRANSCRIPTION REGULATION; YEAST CELL; ANIMAL; GENE SILENCING; GENETIC TRANSCRIPTION; HUMAN; METABOLISM; PHYSIOLOGY; REVIEW;

ANIMALS; GENE SILENCING; HUMANS; PEPTIDYLPROLYL ISOMERASE; RNA POLYMERASE II; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 0036302064     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kvf118     Document Type: Article

References (55)

1. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1
2. Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase
3. Mammalian MAP kinase signalling cascades
4. Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
5. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
6. Signal transduction by the Wnt family of ligands
7. Monoclonal antibodies to mitotic cells
8. The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans
9. 0 arrest
10. Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A
11. The Wnt/Wg signal transducer β-catenin controls fibronectin expression
12. NFAT signalling in vertebrate development
13. Sequence and mutational analysis of ESSI, a gene essential for growth in Saccharomyces cerevisiae
14. Mutations in a peptidyl-cis/trans-isomerase gene lead to a defect in 3′-end formation of a pre-mRNA in Saccharomyces cerevisiae
15. Identification of c-Myc as a target of the APC pathway
16. Curbing the nuclear activities of β-catenin
17. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by Juglone
18. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis
19. Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe
20. Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution
21. Enzyme assembly after de novo synthesis in rabbit reticulocyte lysate involves molecular chaperones and immunophilins
22. The Arabidopsis thaliana Pin1 At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase
23. SUC1 and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope
24. Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism
25. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes
26. Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1
27. A human peptidyl-prolyl isomerase essential for regulation of mitosis
28. The prolyl-isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
29. Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function
30. The dodo gene family encodes a novel protein involved in signal transduction and protein folding
31. Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52
32. Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
33. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution
34. Phosphocarboxyl-terminal domain binding and the role of prolyl isomerase in pre-mRNA 3′-end formation
35. Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin
36. Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR
37. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
38. Side-chain effects on peptidyl-prolyl cis/trans isomerases
39. Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis
40. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly
41. Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC
42. Prolyl isomerases join the fold
43. Chemistry and biology of the immunophilins and their immunosuppressive ligands
44. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
45. Pin1 acts catalytically to promote a conformational change in Cdc25
46. Functions of WW domains in the nucleus
47. β-Catenin regulates expression of cyclin D1 in colon carcinoma cells
48. Identification and characterisation of a 14 kDa human protein as a novel parvulin-like peptidyl-prolyl cis/trans isomerase
49. Atomic structure of FKBP-FK506, an immunophilin-immuno-suppressant complex
50. Structural basis for phosphoserine-proline recognition by group IV WW domains
51. Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase
52. Requirement of the proly1 isomerase Pin1 for the replication checkpoint
53. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery
54. Pin1 is overexpressed in breast cancer and cooperates with Ras signalling in increasing the transcriptional activity of c-Jun towards cyclin D1
55. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and Tau proteins