A Peptide-functionalized polymer as a minimal scaffold protein to enhance cluster formation in early T cell signal transduction
| Autor: | Oda Stoevesandt, Merel J. W. Adjobo-Hermans, Michael D. Sinzinger, Ivo R. Ruttekolk, J. Joris Witsenburg, Günter Roth, Roland Brock |
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| Rok vydání: | 2015 |
| Předmět: |
Scaffold protein
Proline T-Lymphocytes T cell Peptide Biology Biochemistry Jurkat cells SH3 domain src Homology Domains Jurkat Cells Polymethacrylic Acids medicine Humans Binding site Molecular Biology Adaptor Proteins Signal Transducing chemistry.chemical_classification Organic Chemistry Signal transducing adaptor protein Disorders of movement Donders Center for Medical Neuroscience [Radboudumc 3] Cell biology Radboud Institute for Molecular Life Sciences medicine.anatomical_structure chemistry Molecular Medicine Signal transduction Peptides Nanomedicine Radboud Institute for Molecular Life Sciences [Radboudumc 19] Signal Transduction |
| Zdroj: | ChemBioChem, 16, 4, pp. 602-10 ChemBioChem, 16, 602-10 |
| ISSN: | 1439-4227 |
| Popis: | Item does not contain fulltext In cellular signal transduction, scaffold proteins provide binding sites to organize signaling proteins into supramolecular complexes and act as nodes in the signaling network. Furthermore, multivalent interactions between the scaffold and other signaling proteins contribute to the formation of protein microclusters. Such microclusters are prominent in early T cell signaling. Here, we explored the minimal structural requirement for a scaffold protein by coupling multiple copies of a proline-rich peptide corresponding to an interaction motif for the SH3 domain of the adaptor protein GADS to an N-(2-hydroxypropyl)methacrylamide polymer backbone. When added to GADS-containing cell lysates, these scaffolds (but not individual peptides) promoted the binding of GADS to peptide microarrays. This can be explained by the cross-linking of GADS into larger complexes. Furthermore, following import into Jurkat T cell leukemia cells, this synthetic scaffold enhanced the formation of microclusters of signaling proteins. |
| Databáze: | OpenAIRE |
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