Cited by 113Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersProtein Kinase Regulation and GTPase Signaling

C‐terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3

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Boeckers, Tobias M., Liedtke, Thomas, Spilker, Christina, Dresbach, Thomas, Bockmann, Jürgen, Kreutz, Michael R., Gundelfinger, Eckart D.·2005·Journal of Neurochemistry

Abstract

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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  1. Goslin K. and Banker G. (1991) Rat hippocampal neurons in low density culture, in Culturing Nerve Cells (Banker, G. Goslin, K., eds), pp. 251-281. MIT Press, Cambridge MA.

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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
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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