Evidence map›Paper›PMID 25071438›Full record

ArticleFrontiers in molecular neuroscience2014

Neuron-specific protein interactions of Drosophila CASK-β are revealed by mass spectrometry.

Konark Mukherjee, Justin B Slawson, Bethany L Christmann, Leslie C Griffith

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. CASK hypomorph mice display cone photoreceptor dysfunction.bioRxiv : the preprint server for biology · 2026
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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.

Konark MukherjeeDepartment of Biology, Volen Center for Complex Systems, National Center for Behavioral Genomics, Brandeis University Waltham, MA, USA.
Justin B SlawsonDepartment of Biology, Volen Center for Complex Systems, National Center for Behavioral Genomics, Brandeis University Waltham, MA, USA.
Bethany L ChristmannDepartment of Biology, Volen Center for Complex Systems, National Center for Behavioral Genomics, Brandeis University Waltham, MA, USA.
Leslie C GriffithDepartment of Biology, Volen Center for Complex Systems, National Center for Behavioral Genomics, Brandeis University Waltham, MA, USA.
Brandeis University · US

Funding

NEUROSCIENCE: FROM CHANNELS TO BEHAVIORT32MH019929 · NIMH · BRANDEIS UNIVERSITY · PI GRIFFITH, LESLIE C · 1994 to 2023
$8.5M
GENETIC AND BIOCHEMICAL MECHANISMS OF REGULATIONT32GM007122 · NIGMS · BRANDEIS UNIVERSITY · PI LOVETT, SUSAN THOMAS · 1985 to 2020
$7.5M
NEUROCHEMISTRY AND GENETICS OF DROSOPHILA CAM KINASE IIR01GM054408 · NIGMS · BRANDEIS UNIVERSITY · PI GRIFFITH, LESLIE C · 1996 to 2014
$5.0M
The Behavioral Role and Synpatic Localization of dCASK in Drosophila melanogasterF31NS064679 · NINDS · BRANDEIS UNIVERSITY · PI SLAWSON, JUSTIN · 2009 to 2011
$58k
Investigating the cellular basis of memory consolidation in DrosophilaF31NS086764 · NINDS · BRANDEIS UNIVERSITY · PI CHRISTMANN, BETHANY L · 2013 to 2014
$51k
NIGMS NIH HHS R01 GM054408NIGMS NIH HHS T32 GM007122NIMH NIH HHS T32 MH019929NINDS NIH HHS F31 NS064679NINDS NIH HHS F31 NS086764
6 · The paper itself

Abstract

Modular scaffolding proteins are designed to have multiple interactors. CASK, a member of the membrane-associated guanylate kinase (MAGUK) superfamily, has been shown to have roles in many tissues, including neurons and epithelia. It is likely that the set of proteins it interacts with is different in each of these diverse tissues. In this study we asked if within the Drosophila central nervous system, there were neuron-specific sets of CASK-interacting proteins. A YFP-tagged CASK-β transgene was expressed in genetically defined subsets of neurons in the Drosophila brain known to be important for CASK function, and proteins present in an anti-GFP immunoprecipitation were identified by mass spectrometry. Each subset of neurons had a distinct set of interacting proteins, suggesting that CASK participates in multiple protein networks and that these networks may be different in different neuronal circuits. One common set of proteins was associated with mitochondria, and we show here that endogenous CASK-β co-purifies with mitochondria. We also determined CASK-β posttranslational modifications for one cell type, supporting the idea that this technique can be used to assess cell- and circuit-specific protein modifications as well as protein interaction networks.

Indexed as

CASKDrosophilaGAL4/UASimmunoprecipitationMAGUKmass spectrometry

Identifiers

PMID25071438
PMCPMC4075472
OpenAlexW2022564110

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.