Phosphoserine/threonine-binding domains

Phosphorylation of proteins on serine and threonine residues has traditionally been viewed as a means to allosterically regulate catalytic activity. Research within the past five years, however, has revealed that serine/threonine phosphorylation can also directly result in the formation of multimole...

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Bibliographic Details
Published inCurrent Opinion in Cell Biology Vol. 13; no. 2; pp. 131 - 138
Main Authors Yaffe, Michael B, Elia, Andrew E.H
Format Book Review Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.2001
Subjects
14-3-3
Animals
Binding Sites
F-box
forkhead-associated domain
Humans
Phosphoproteins - chemistry
Phosphoproteins - metabolism
Phosphorylation
phosphoserine
Phosphoserine - metabolism
Phosphothreonine - metabolism
phosphotyrosine
Protein Structure, Tertiary
signal transduction
WD40
WW domains
phosphotyrosine
14-3-3
WD40
F-box
signal transduction
Cell biology
WW domains
phosphorylation
phosphoserine
forkhead-associated domain
Structural biology
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Summary:Phosphorylation of proteins on serine and threonine residues has traditionally been viewed as a means to allosterically regulate catalytic activity. Research within the past five years, however, has revealed that serine/threonine phosphorylation can also directly result in the formation of multimolecular signaling complexes through specific interactions between phosphoserine/threonine (pSer/Thr)-binding modules and phosphorylated sequence motifs. pSer/Thr-binding proteins and domains currently include 14-3-3, WW domains, forkhead-associated domains, and, tentatively, WD40 repeats and leucine-rich regions. It seems likely that additional modules will be found in the future. The amino acid sequences recognized by these pSer/Thr-binding modules show partial overlap with the optimal phosphorylation motifs for different protein kinase subfamilies, allowing the formation of specific signaling complexes to be controlled through combinatorial interactions between particular upstream kinases and a particular binding module. The structural basis for pSer/Thr binding differs dramatically between 14-3-3 proteins, WW domains and forkhead-associated domains, suggesting that their pSer/Thr binding function was acquired through convergent evolution.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0955-0674
1879-0410
DOI:10.1016/S0955-0674(00)00189-7