Evidence map›Paper›PMID 35602601›Full record

ArticleFrontiers in cell and developmental biology2022

Proteomic Identification of Phosphorylation-Dependent Septin 7 Interactors that Drive Dendritic Spine Formation.

Sujin Byeon, Bailey Werner, Reilly Falter, Kristian Davidsen, Calvin Snyder, Shao-En Ong, Smita Yadav

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024
    Article
  7. Article
  8. Review
  9. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Sujin ByeonGraduate Program in Neuroscience, University of Washington, Seattle, WA, United States.
Bailey WernerDepartment of Pharmacology, University of Washington, Seattle, WA, United States.
Reilly FalterDepartment of Pharmacology, University of Washington, Seattle, WA, United States.
Kristian DavidsenHuman Biology Division, Fred Hutchinson Cancer Research Center, Seattle, WA, United States.
Calvin SnyderDepartment of Pharmacology, University of Washington, Seattle, WA, United States.
Shao-En OngDepartment of Pharmacology, University of Washington, Seattle, WA, United States.
Smita YadavDepartment of Pharmacology, University of Washington, Seattle, WA, United States.
University of Washington · USFred Hutch Cancer Center · US

Funding

TAOK2 Kinase Signaling in Human Neural Stem Cell DevelopmentR01MH121674 · NIMH · UNIVERSITY OF WASHINGTON · PI YADAV, SMITA · 2020 to 2024
$2.2M
Supplement to DEFINING PATHWAY-SPECIFIC KINASE SIGNALING MODULES WITH PROTEOMICSR01GM129090 · NIGMS · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2019 to 2022
$1.7M
A NanoLC-Orbitrap Tribrid Instrument for Comprehensive Proteomics AnalysesS10OD021502 · OD · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2017 to 2017
$906k
Role of Autism Susceptibility Gene, TAOK2 kinase, and its novel substrates in SynaptogenesisR00MH108648 · NIMH · UNIVERSITY OF WASHINGTON · PI YADAV, SMITA · 2018 to 2020
$745k
NIGMS NIH HHS R01 GM129090NIH HHS S10 OD021502NIMH NIH HHS R00 MH108648NIMH NIH HHS R01 MH121674
6 · The paper itself

Abstract

Septins are a family of cytoskeletal proteins that regulate several important aspects of neuronal development. Septin 7 (Sept7) is enriched at the base of dendritic spines in excitatory neurons and mediates both spine formation and spine and synapse maturation. Phosphorylation at a conserved C-terminal tail residue of Sept7 mediates its translocation into the dendritic spine head to allow spine and synapse maturation. The mechanistic basis for postsynaptic stability and compartmentalization conferred by phosphorylated Sept7, however, is unclear. We report herein the proteomic identification of Sept7 phosphorylation-dependent neuronal interactors. Using Sept7 C-terminal phosphopeptide pulldown and biochemical assays, we show that the 14-3-3 family of proteins specifically interacts with Sept7 when phosphorylated at the T426 residue. Biochemically, we validate the interaction between Sept7 and 14-3-3 isoform gamma and show that 14-3-3 gamma is also enriched in the mature dendritic spine head. Furthermore, we demonstrate that interaction of phosphorylated Sept7 with 14-3-3 protects it from dephosphorylation, as expression of a 14-3-3 antagonist significantly decreases phosphorylated Sept7 in neurons. This study identifies 14-3-3 proteins as an important physiological regulator of Sept7 function in neuronal development.

Indexed as

14-3-3dendritic spinesphosphoregulationproteomicsseptin

Identifiers

PMID35602601
PMCPMC9114808
OpenAlexW4225418340

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.