Evidence map›Paper›PMID 19472188›Full record

ArticleDevelopmental neurobiology2009

A critical step for postsynaptic F-actin organization: regulation of Baz/Par-3 localization by aPKC and PTEN.

Preethi Ramachandran, Romina Barria, James Ashley, Vivian Budnik

Open access · greenAbstract read
In one paragraph

Article in Developmental neurobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

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  4. Immunohistochemical Analysis of the Drosophila Larval Neuromuscular Junction.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  6. The Roles of Par3, Par6, and aPKC Polarity Proteins in Normal Neurodevelopment and in Neurodegenerative and Neuropsychiatric Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Review
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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

4 authors at 1 institution in 1 country.

Preethi RamachandranDepartment of Neurobiology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Romina Barria
James Ashley
Vivian Budnik
University of Massachusetts Chan Medical School · US

Funding

PILOT AND FEASIBILITY PROGRAMP30DK032520 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CZECH, MICHAEL P · 1986 to 2010
$14.6M
The Wingless Transduction Pathway in Synapse DevelopmentR01MH070000 · NIMH · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BUDNIK, VIVIAN G. · 2004 to 2013
$3.6M
MORPHOLOGICAL PLASTICITY AT THE NEUROMUSCULAR JUNCTIONR01NS030072 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BUDNIK, VIVIAN G. · 1992 to 2009
$2.7M
NIDDK NIH HHS DK32520NIDDK NIH HHS P30 DK032520NIMH NIH HHS R01 MH070000NINDS NIH HHS R01 NS030072
6 · The paper itself

Abstract

Actin remodeling has emerged as a critical process during synapse development and plasticity. Thus, understanding the regulatory mechanisms controlling actin organization at synapses is exceedingly important. Here, we used the highly plastic Drosophila neuromuscular junction (NMJ) to understand mechanisms of actin remodeling at postsynaptic sites. Previous studies have suggested that the actin-binding proteins Spectrin and Coracle play a critical role in NMJ development and the anchoring of glutamate receptors most likely through actin regulation. Here, we show that an additional determinant of actin organization at the postsynaptic region is the PDZ protein Baz/Par-3. Decreasing Baz levels in postsynaptic muscles has dramatic consequences for the size of F-actin and spectrin domains at the postsynaptic region. In turn, proper localization of Baz at this site depends on both phosphorylation and dephosphorylation events. Baz phosphorylation by its binding partner, atypical protein kinase C (aPKC), is required for normal Baz targeting to the postsynaptic region. However, the retention of Baz at this site depends on its dephosphorylation mediated by the lipid and protein phosphatase PTEN. Misregulation of the phosphorylation state of Baz by genetic alterations in PTEN or aPKC activity has detrimental consequences for postsynaptic F-actin and spectrin localization, synaptic growth, and receptor localization. Our results provide a novel mechanism of postsynaptic actin regulation through Baz, governed by the antagonistic actions of aPKC and PTEN. Given the conservation of these proteins from worms to mammals, these results are likely to provide new insight into actin organization pathways. (c) 2009 Wiley Periodicals, Inc. Develop Neurobiol 2009.

Indexed as

ActinsAnimalsAnimals, Genetically ModifiedDrosophilaDrosophila ProteinsGene Expression Regulation, DevelopmentalHorseradish PeroxidaseIntracellular Signaling Peptides and ProteinsMicroscopy, Electron, TransmissionModels, BiologicalNeuromuscular JunctionProtein Kinase CPTEN PhosphohydrolaseRadiotherapy, ConformalRNA InterferenceSpectrinActinsbaz protein, DrosophilaDrosophila ProteinsHorseradish PeroxidaseIntracellular Signaling Peptides and ProteinsPKC-3 proteinProtein Kinase CPTEN PhosphohydrolasePTEN protein, DrosophilaSpectrin

Identifiers

PMID19472188
PMCPMC2885019
OpenAlexW2089985516

What OpenQuestion holds

Textmetadata
LicenceTDM
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.