Evidence map›Paper›PMID 36264429›Full record

ArticleCellular and molecular life sciences : CMLS2022

Functional interdependence of the actin regulators CAP1 and cofilin1 in control of dendritic spine morphology.

Anika Heinze, Cara Schuldt, Sharof Khudayberdiev, Bas van Bommel, Daniela Hacker, Toni G Schulz, Ramona Stringhi, Elena Marcello, Marina Mikhaylova, Marco B Rust

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Anika HeinzeMolecular Neurobiology Group, Institute of Physiological Chemistry, Philipps-University of Marburg, 35032, Marburg, Germany.
Cara SchuldtMolecular Neurobiology Group, Institute of Physiological Chemistry, Philipps-University of Marburg, 35032, Marburg, Germany.
Sharof KhudayberdievMolecular Neurobiology Group, Institute of Physiological Chemistry, Philipps-University of Marburg, 35032, Marburg, Germany.
Bas van BommelAG Optobiology, Institute of Biology, Humboldt-University, 10115, Berlin, Germany.
Daniela HackerAG Optobiology, Institute of Biology, Humboldt-University, 10115, Berlin, Germany.
Toni G SchulzMolecular Neurobiology Group, Institute of Physiological Chemistry, Philipps-University of Marburg, 35032, Marburg, Germany.
Ramona StringhiDepartment of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, 20133, Milan, Italy.
Elena MarcelloDepartment of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, 20133, Milan, Italy.
Marina MikhaylovaAG Optobiology, Institute of Biology, Humboldt-University, 10115, Berlin, Germany.
Marco B RustMolecular Neurobiology Group, Institute of Physiological Chemistry, Philipps-University of Marburg, 35032, Marburg, Germany. marco.rust@staff.uni-marburg.de.ORCID http://orcid.org/0000-0003-2737-1250
Philipps University of Marburg · DEUniversität Hamburg · DEUniversity of Milan · ITHumboldt-Universität zu Berlin · DE

Funding

Deutsche Forschungsgemeinschaft MI1923/1-2Deutsche Forschungsgemeinschaft RU 1232/7-1
6 · The paper itself

Abstract

The vast majority of excitatory synapses are formed on small dendritic protrusions termed dendritic spines. Dendritic spines vary in size and density that are crucial determinants of excitatory synaptic transmission. Aberrations in spine morphogenesis can compromise brain function and have been associated with neuropsychiatric disorders. Actin filaments (F-actin) are the major structural component of dendritic spines, and therefore, actin-binding proteins (ABP) that control F-actin dis-/assembly moved into the focus as critical regulators of brain function. Studies of the past decade identified the ABP cofilin1 as a key regulator of spine morphology, synaptic transmission, and behavior, and they emphasized the necessity for a tight control of cofilin1 to ensure proper brain function. Here, we report spine enrichment of cyclase-associated protein 1 (CAP1), a conserved multidomain protein with largely unknown physiological functions. Super-resolution microscopy and live cell imaging of CAP1-deficient hippocampal neurons revealed impaired synaptic F-actin organization and dynamics associated with alterations in spine morphology. Mechanistically, we found that CAP1 cooperates with cofilin1 in spines and that its helical folded domain is relevant for this interaction. Moreover, our data proved functional interdependence of CAP1 and cofilin1 in control of spine morphology. In summary, we identified CAP1 as a novel regulator of the postsynaptic actin cytoskeleton that is essential for synaptic cofilin1 activity.

Indexed as

ActinsDendritic SpinesActin CytoskeletonMicrofilament ProteinsOligopeptidesSynapsesSynapsinsActinsCAP1-6DMicrofilament ProteinsOligopeptidesSynapsinsActin dynamicsActin turnoverPostsynaptic densitySynaptic actinSynaptic plasticity

Identifiers

PMID36264429
PMCPMC9585016
OpenAlexW4306884852

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.