The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
C‐terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3
Open accessAbstract
Synapses are specialized contact sites mediating communication between neurons. Synaptogenesis requires the specific assembly of protein clusters at both sides of the synaptic contact by mechanisms that are barely understood. We studied the synaptic targeting of multi‐domain proteins of the ProSAP/Shank family thought to serve as master scaffolding molecules of the postsynaptic density. In contrast to Shank1, expression of green‐fluorescent protein (GFP)‐tagged ProSAP1/Shank2 and ProSAP2/Shank3 deletion constructs in hippocampal neurons revealed that their postsynaptic localization relies on the integrity of the C‐termini. The shortest construct that was perfectly targeted to synaptic sites included the last 417 amino acids of ProSAP1/Shank2 and included the C‐terminal sterile alpha motif (SAM) domain. Removal of 54 residues from the N‐terminus of this construct resulted in a diffuse distribution in the cytoplasm. Altogether, our data delineate a hitherto unknown targeting signal in both ProSAP1/Shank2 and ProSAP2/Shank3 and provide evidence for an implication of these proteins and their close homologue, Shank1, in distinct molecular pathways.
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“These results are consistent with previous data showing that the Homer-binding site is involved in the synaptic localization of Shank3.22, 31”
From SHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism (2012) · cites this paper as [31]
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“Shank3WT overexpression led to an accumulation of the protein in dendritic spines (Figure 2a), as previously reported.31”
From SHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism (2012) · cites this paper as [31]
In the citing paper
“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 Boeckers et al., 2005
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PDZ Domains and the Organization of Supramolecular Complexes
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Coupling of mGluR/Homer and PSD-95 Complexes by the Shank Family of Postsynaptic Density Proteins
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Self-citationCharacterization of the Shank Family of Synaptic Proteins
Lim, S., Naisbitt, S., Yoon, J., Hwang, J.-I., Suh, P.-G., Sheng, M., & Kim, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29510 · Cited by 295
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Self-citationDu, Y., Weed, S. A., Xiong, W.-C., Marshall, T. D., & Parsons, J. T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5838 · Cited by 254
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Self-citationMAGUKs in synapse assembly and function: an emerging view
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Research works printed but not linked: 1
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Cited by
Sorted by citations
SHANK proteins: roles at the synapse and in autism spectrum disorder
Monteiro, P., & Feng, G. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.183 · Cited by 681
Mutations in the SHANK2 synaptic scaffolding gene in autism spectrum disorder and mental retardation
Berkel, S., Marshall, C. R., Weiss, B., Howe, J., Roeth, R., Moog, U., Endris, V., Roberts, W., Szatmari, P., Pinto, D., et al. (2010) · Nature Genetics · doi:10.1038/ng.589 · Cited by 563
Modeling Autism by SHANK Gene Mutations in Mice
Jiang, Y.-H., & Ehlers, M. D. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.016 · Cited by 488
Leblond, C. S., Heinrich, J., Delorme, R., Proepper, C., Betancur, C., Huguet, G., Konyukh, M., Chaste, P., Ey, E., Rastam, M., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002521 · Cited by 429
Self-citationThe postsynaptic density proteins Homer and Shank form a polymeric network structure
Hayashi, M. K., Tang, C., Verpelli, C., Narayanan, R., Stearns, M. H., Xu, R.-M., Li, H., Sala, C., & Hayashi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.01.050 · Cited by 356
Metadata
- Authors
- Boeckers, T. M., Liedtke, T., Spilker, C., Dresbach, T., Bockmann, J., Kreutz, M. R., & Gundelfinger, E. D.
- Affiliations
- Universität Ulm (DE)
- University of Münster (DE)
- Leibniz Institute for Neurobiology (DE)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2004-12-23
- Volume
- 92
- Issue
- 3
- Pages
- 519-524
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2099448375
- Cited by
- 113
- References
- 20
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 7 · 2022: 9 · 2021: 9 · 2020: 9 · 2019: 1 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 12 · 2014: 1 · 2013: 5 · 2012: 4
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Centre National de la Recherche Scientifique
- 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 Kinase Regulation and GTPase Signaling
- Keywords
- Shank1, postsynaptic density, synaptic targeting, sterile alpha motif domain, synaptic scaffolding proteins, synaptogenesis, hippocampal neurons, protein localization
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cells, Cultured, Molecular Sequence Data, Nerve Tissue Proteins, Recombinant Fusion Proteins, Synapses, Transfection, Sequence Deletion, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Rats
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