On the role of acylation of transmembrane proteins
Acylation is a frequent means to ensure membrane association of a variety of soluble proteins in living cells. However, many transmembrane proteins are palmitoylated, indicating that this posttranslational modification may also serve as a means to regulate protein trafficking. Based on coarse-graine...
Gespeichert in:
| Hauptverfasser: | , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
26 February 2010
|
| In: |
Biophysical journal
Year: 2010, Jahrgang: 98, Heft: 5, Pages: 800-804 |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2009.11.014 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.bpj.2009.11.014 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0006349509017421 
|
| Verfasserangaben: | Diana Morozova and Matthias Weiss |
| Zusammenfassung: | Acylation is a frequent means to ensure membrane association of a variety of soluble proteins in living cells. However, many transmembrane proteins are palmitoylated, indicating that this posttranslational modification may also serve as a means to regulate protein trafficking. Based on coarse-grained membrane simulations, we find that protein acylation significantly alters the tilting of transmembrane proteins with respect to the bilayer normal. In addition, the proteins' partitioning behavior and cluster formation ability due to hydrophobic mismatching is strongly altered. Based on our results, we propose that acylation is a potent means to regulate the trafficking of transmembrane proteins along the early secretory pathway. |
|---|---|
| Beschreibung: | Gesehen am 04.05.2023 |
| Beschreibung: | Online Resource |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2009.11.014 |