First-pass extracted concept

14-3-3 proteins

Candidate: concept label1 source documents3 linked claims

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Aliases

14-3-3 family of proteins, 14-3-3s

Extracted Explainers

What the tool is doing

14-3-3 proteins bind specifically phosphorylated proteins and complete kinase-induced transitions in target activity or localization. In the review abstract, they are presented as regulators of signal flux in plant signaling pathways including photoperiodic flowering.

Source 1DOI PubMed

Resources required

The abstract states that well characterized 14-3-3 genetic tools in sufficient diversity were needed to tie 14-3-3 interactions to light signaling and flowering.

Source 1DOI PubMed

What problem it solves

They provide a mechanism for coupling phosphorylation state to changes in protein activity, localization, and pathway output.

Source 1DOI PubMed

What it does not solve

The abstract emphasizes that overlapping and isoform-specific roles confound functional dissection, so the family does not by itself resolve which specific 14-3-3 member controls each flowering or light-signaling step.

Source 1DOI PubMed

Alternatives

No direct alternative toolkit is named in the abstract; instead, the source contrasts 14-3-3 regulation with broader mechanisms such as localization, phosphorylation, and regulated proteolysis.

Source 1DOI PubMed

Evidence Snippets

The 14-3-3 family of proteins is well known for participating in signal transduction by binding specifically phosphorylated proteins, thereby completing their kinase-induced transition in activity or localization.

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2008Plant Signaling & BehaviorDOI PubMed

1 evidence snippet 3 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1mechanistic alignmentsupports2008Source 1DOI PubMed

Key control points in the photoperiod pathway involve accumulation, localization, and stability of critical protein factors, and these mechanisms align with processes regulated by 14-3-3 proteins in other systems.

Quoted textsource-backed

There are pivotal points in the photoperiod pathway that are characterized by the accumulation, localization and stability of critical protein factors, all of which are strongly affected by light quality and photoperiod duration. These mechanisms (localization, phosphorylation, regulated proteolysis) are the same as those regulated by 14-3-3 proteins in other systems.

Claim 2mechanistic rolesupports2008Source 1DOI PubMed

14-3-3 proteins participate in signal transduction by binding specifically phosphorylated proteins and completing kinase-induced transitions in target activity or localization.

Quoted textsource-backed

The 14-3-3 family of proteins is well known for participating in signal transduction by binding specifically phosphorylated proteins, thereby completing their kinase-induced transition in activity or localization.

Claim 3pathway involvementsupports2008Source 1DOI PubMed

Studies in Arabidopsis thaliana have described that 14-3-3 proteins functionally affect fundamental plant signal transduction pathways including the photoperiodic flowering pathway.

Quoted textsource-backed

Only recently, however, have studies in Arabidopsis thaliana described that some of the most fundamental plant signal transduction pathways, including the photoperiodic flowering pathway, are functionally affected by 14-3-3s.