Phosphoserine/threonine-binding domains

Current Opinion in Cell Biology

Volumn 13, Issue 2, 2001, Pages 131-138

  Yaffe, Michael B ^a,b   Elia, Andrew E H ^b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PHOSPHOSERINE; PHOSPHOSERINE THREONINE BINDING PROTEIN; THREONINE; UNCLASSIFIED DRUG;

ALLOSTERISM; AMINO ACID SEQUENCE; BINDING AFFINITY; BINDING SITE; CATALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; REVIEW; SCHIZOSACCHAROMYCES POMBE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

SCHIZOSACCHAROMYCES POMBE;

EID: 0035313699     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00189-7     Document Type: Review

References (84)

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5. 14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast
6. Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
7. Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
8. DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding
9. Maintenance of G2 arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import
10. Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25
11. Nuclear localization of cdc25 is regulated by DNA damage and a 14-3-3 protein
12. Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site
13. 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts
14. 14-3-3σ is a p53-regulated inhibitor of G2/M progression
15. 14-3-3σ is required to prevent mitotic catastrophe after DNA damage
16. High frequency of hypermethylation at the 14-3-3 sigma locus leads to gene silencing in breast cancer
17. 14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo
18. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
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20. 14-3-3 proteins block apoptosis and differentially regulate MAPK cascades
21. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
22. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X
23. Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155
24. BAD Ser155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
25. Regulation of BAD by cAMP dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
26. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
27. Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins
28. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
29. The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors
30. TAZ; a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ-domain proteins
31. Association of the TLX-2 homeodomain and 14-3-3η signaling proteins
32. Purification and properties of the Xenopus Hat1 acetyltransferase: Association with the 14-3-3 proteins in the oocyte nucleus
33. Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
34. Regulation of histone deacetylase 4 by binding of 14-3-3 proteins
35. Modulation of human DNA topoisomerase IIalpha function by interaction with 14-3-3epsilon
36. Involvement of 14-3-3 proteins in nuclear localization of telomerase
37. Function of WW domains as phosphoserine- or phosphothreonine-binding modules
38. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and Tau proteins
39. Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-End formation
40. Structural basis for phosphoserine-proline recognition by group IV WW domains
41. The FHA domain: A putative nuclear signalling domain found in protein kinases and transcription factors
42. Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain
43. Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53
44. FHA domain boundaries of the dun1p and rad53p cell cycle checkpoint kinases
45. II. Structure and specificity of the interaction between the FHA2 domain of rad53 and phosphotyrosyl peptides
46. The molecular basis of FHA domain: Phosphopeptide binding specificity and implications for phosphodependent signaling mechanisms
47. Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
48. Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
49. The FHA domain is a modular phosphopeptide recognition motif
50. Heterozygous germ line hCHK2 mutations in Li-Fraumeni syndrome
51. Chfr defines a mitotic stress checkpoint that delays entry into metaphase
52. The forkhead-associated domain of Ki-67 antigen interacts with the novel kinesin-like protein Hklp2
53. NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry
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58. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
59. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
60. Identification of the receptor component of the IκBα-ubiquitin ligase
61. Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP
62. HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IκBα and beta-catenin
63. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα
64. SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-κB p105 requires phosphorylation of its C-terminus by IκB kinase
65. The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell
66. β-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation
67. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
68. Sud1(+) targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1 proteins for degradation and stops unwanted diploidization in fission yeast
69. Regulation of the replication initiator protein p65cdc18 by CDK phosphorylation
70. An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of β-catenin
71. A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
72. An essential function of Grr1 for the degradation of Cln2 is to act as a binding core that links Cln2 to Skp1
73. Inhibition of NF-κ-B cellular function via specific targeting of the I-κ-B-ubiquitin ligase
74. The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
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76. Molecular dissection of the interactions among IκBα, FWD1, and Skp1 required for ubiquitin-mediated proteolysis of IκBα
77. p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
78. Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
79. Phosphorylation controls timing of Cdc6p destruction: A biochemical analysis
80. Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation
81. A structural basis of the interactions between leucine-rich repeats and protein ligands
82. Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
83. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
84. Insights into SCF ubiquitin ligase from the structure of the Skp1-Skp2 complex