UNC119A Decreases the Membrane Binding of Myristoylated c-Src
| Autor: | Nelli Erwin, Mridula Dwivedi, Herbert Waldmann, Tom Mejuch, Roland Winter |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Cell signaling 010405 organic chemistry Chemistry Vesicle Organic Chemistry Peptide 01 natural sciences Biochemistry 0104 chemical sciences 03 medical and health sciences 030104 developmental biology Förster resonance energy transfer Membrane Cytoplasm Biophysics Molecular Medicine lipids (amino acids peptides and proteins) Molecular Biology Proto-oncogene tyrosine-protein kinase Src Myristoylation |
| Zdroj: | Chembiochem : a European journal of chemical biology. 19(14) |
| ISSN: | 1439-7633 |
| Popis: | Plasma membrane localization of myristoylated c-Src, a proto-oncogene protein-tyrosine kinase, is required for its signaling activity. Recent studies proposed that UNC119 protein functions as a solubilizing factor for myristoylated proteins, thereby regulating their subcellular distribution and signaling. The underlying molecular mechanism by which UNC119 regulates the membrane binding of c-Src has remained elusive. By combining different biophysical techniques, we have found that binding of a myristoylated c-Src-derived N-terminal peptide (Myr-Src) by UNC119A results in a reduced membrane binding affinity of the peptide, due to the competition of binding to membranes. The dissociation of Myr-Src from membranes is facilitated in the presence of UNC119A, as a consequence of which the clustering propensity of this peptide on the membrane is partially impaired. By these means, UNC119A is able to regulate c-Src spatially in the cytoplasm and on cellular membranes, and this has important implications for its cellular signaling. |
| Databáze: | OpenAIRE |
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