The postsynaptic density proteins Homer and Shank form a polymeric network structure
Open accessAbstract
The postsynaptic density (PSD) is crucial for synaptic functions, but the molecular architecture retaining its structure and components remains elusive. Homer and Shank are among the most abundant scaffolding proteins in the PSD, working synergistically for maturation of dendritic spines. Here, we demonstrate that Homer and Shank, together, form a mesh-like matrix structure. Crystallographic analysis of this region revealed a pair of parallel dimeric coiled coils intercalated in a tail-to-tail fashion to form a tetramer, giving rise to the unique configuration of a pair of N-terminal EVH1 domains at each end of the coiled coil. In neurons, the tetramerization is required for structural integrity of the dendritic spines and recruitment of proteins to synapses. We propose that the Homer-Shank complex serves as a structural framework and as an assembly platform for other PSD proteins.
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Deeper within the PSD, Shank and Homer proteins self-assemble into a mesh-like matrix characterized by tetrameric coiled-coils, with Homer located 30-100 nm from the postsynaptic membrane and mGluRs concentrated at peri-PSD locations within 60 nm of the edge.
“Deeper within the PSD, in a region often referred to as the “pallium,” Shank and Homer proteins self-assemble into a mesh-like matrix characterized by tetrameric coiled-coils [42]. Immunogold electron microscopy places Homer in a layer 30–100 nm from the postsynaptic membrane, whereas mGluRs are concentrated at peri-PSD locations within 60 nm of the edge [43].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [42]
Split into 2 atoms — 0 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredHomer1 and Shank1 form a mesh-like matrix thought to function as an organizing lattice for PSD proteins.
“Homer1 and Shank1 form a mesh-like matrix that is thought to function as an organizing lattice for PSD proteins (Hayashi et al., 2009).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Hayashi et al., 2009
Shank3 forms multimers via its C-terminal SAM domain and its PDZ domain.
“Shank3 forms multimers via its C terminal SAM domain (Boeckers et al., 2005; Hayashi et al., 2009; Naisbitt et al., 1999) as well as its PDZ domain (Iskenderian-Epps and Imperiali, 2010).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Hayashi et al., 2009
Because each protein domain mediates a unique set of protein-protein interactions, each Shank3 isoform likely has a distinct set of functions.
“Because each protein domain mediates a unique complement of protein-protein interactions (Hayashi et al., 2009; Roussignol et al., 2005), it is likely that each Shank3 isoform has a distinct set of functions.”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Hayashi et al., 2009
Homer family members regulate diverse synaptic functions.
“Among the various Shank binding proteins, Homer family members have been shown to regulate diverse synaptic functions (Hayashi et al., 2009; Sala et al., 2001; Tu et al., 1999).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Hayashi et al., 2009
Changes in Homer1 and Shank3 across several mouse lines and brain regions are consistent with the known multimeric network formed between these two proteins.
“The corresponding changes of Homer1 and Shank3 in several mouse lines and several brain regions are consistent with the known multimeric network formed between these two proteins (Hayashi et al., 2009; Tu et al., 1999).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Hayashi et al., 2009
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“This organization serves as a structural framework and an assembly platform for other PSD proteins, including GKAP [42].”
- Authors
- Hayashi, M. K., Tang, C., Verpelli, C., Narayanan, R., Stearns, M. H., Xu, R.-M., Li, H., Sala, C., & Hayashi, Y.
- Affiliations
- RIKEN Center for Brain Science (JP)
- Brookhaven National Laboratory (US)
- University of Milan (IT)
- Massachusetts Institute of Technology (US)
- New York University (US)
- Corresponding author
- Hayashi, Mariko Kato
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-04
- Volume
- 137
- Issue
- 1
- Pages
- 159-171
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2680917
- OpenAlex
- W2117421244
- Cited by
- 356
- References
- 35
- Citations by year
- 2026: 15 · 2025: 17 · 2024: 10 · 2023: 11 · 2022: 24 · 2021: 35 · 2020: 21 · 2019: 26 · 2018: 24 · 2017: 26 · 2016: 30 · 2015: 17 · 2014: 20 · 2013: 18 · 2012: 26
- FWCI
- 8.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p50gm068762-10)
- National Institute on Drug Abuse (R01DA017310)
- National Institute of General Medical Sciences (GM 68762, P50-GM068762)
- 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 › Molecular Biology › Protein Structure and Dynamics
- Keywords
- Homer, shank, postsynaptic density, dendritic spines, synaptic scaffolding proteins, protein tetramerization, coiled coil, EVH1 domain, protein network structure, synapse assembly
- MeSH terms
- Homer Scaffolding Proteins, Disks Large Homolog 4 Protein, Animals, Carrier Proteins, Humans, Membrane Proteins, Models, Molecular, Nerve Tissue Proteins, Neurons, Synapses, Crystallography, X-Ray, Intracellular Signaling Peptides and Proteins, Rats
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