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Cited by 24Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersCellular Mechanics and Interactions

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

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Heinze, Anika, Schuldt, Cara, Khudayberdiev, Sharof, van Bommel, Bas, Hacker, Daniela, Schulz, Toni G., Stringhi, Ramona, Marcello, Elena +2 more·2022·Cellular and Molecular Life Sciences
DOI 10.1007/s00018-022-04593-8PMC PMC9585016
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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.

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Authors
Heinze, A., Schuldt, C., Khudayberdiev, S., van Bommel, B., Hacker, D., Schulz, T. G., Stringhi, R., Marcello, E., Mikhaylova, M., & Rust, M. B.
Affiliations
  • Philipps University of Marburg (DE)
  • Humboldt-Universität zu Berlin (DE)
  • University of Milan (IT)
Corresponding author
Rust, Marco B.
ORCID
Venue
Cellular and Molecular Life Sciences
Publisher
Springer Science and Business Media LLC
Published
2022-10-20
Volume
79
Issue
11
Pages
558-558
ISSN
  • 1420-682X (ISSN-L)
  • 1420-9071
DOI
10.1007/s00018-022-04593-8
PMC
PMC9585016
OpenAlex
W4306884852
Cited by
24
References
7
Citations by year
2026: 8 · 2025: 4 · 2024: 7 · 2023: 5
FWCI
1.77
Type
journal article
Language
en
Update notices
correction (2024-01-18)
Open access
Licence
Locations
  • Cellular and Molecular Life Sciences (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
Funders
  • Deutsche Forschungsgemeinschaft (RU 1232/10-1, MI1923/1-2)
  • Philipps-Universität Marburg
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
CAP1, cofilin-1, dendritic spine morphology, actin cytoskeleton, F-actin dynamics, actin-binding proteins, postsynaptic spines, hippocampal neurons, synaptic plasticity, neuropsychiatric disorders
MeSH terms
Actins, Microfilament Proteins, Actin Cytoskeleton, Oligopeptides, Synapses, Synapsins, Dendritic Spines

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