Abstract:
:14-3-3 proteins were the first signaling molecules to be identified as discrete phosphoserine/threonine binding modules. This family of proteins, which includes seven isotypes in human cells and up to 15 in plants, plays critical roles in cell signaling events that control progress through the cell cycle, transcriptional alterations in response to environmental cues, and programmed cell death. Despite over 30 years of research, distinct roles for most isotypes remain unknown. Though 14-3-3 proteins perform different functions for different ligands, general mechanisms of 14-3-3 action include changes in activity of bound ligands, altered association of bound ligands with other cellular components, and changes in intracellular localization of 14-3-3-bound cargo. We present a speculative model where binding of 14-3-3 to multiple sites on some ligands results in global ligand conformational changes that mediate their biological effects. For these multi-site ligands, one binding site is likely to function as a 'gatekeeper' whose phosphorylation is necessary for 14-3-3 binding but may not always be sufficient for full biological activity. If correct, then 14-3-3 may prove to be a bona fide phosphodependent signaling chaperone.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Yaffe MBdoi
10.1016/s0014-5793(01)03288-4keywords:
subject
Has Abstractpub_date
2002-02-20 00:00:00pages
53-7issue
1eissn
0014-5793issn
1873-3468pii
S0014579301032884journal_volume
513pub_type
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