dc.creator | Chumpen Ramirez, Sabrina Vanesa | |
dc.creator | Astrada, Micaela R. | |
dc.creator | Daniotti, Jose Luis | |
dc.date.accessioned | 2021-04-05T15:32:09Z | |
dc.date.accessioned | 2022-10-15T09:49:10Z | |
dc.date.available | 2021-04-05T15:32:09Z | |
dc.date.available | 2022-10-15T09:49:10Z | |
dc.date.created | 2021-04-05T15:32:09Z | |
dc.date.issued | 2020-01 | |
dc.identifier | Chumpen Ramirez, Sabrina Vanesa; Astrada, Micaela R.; Daniotti, Jose Luis; PtdIns4P-mediated electrostatic forces influence S-acylation of peripheral proteins at the Golgi complex; Portland Press; Bioscience Reports; 40; 1; 1-2020; 1-19 | |
dc.identifier | 0144-8463 | |
dc.identifier | http://hdl.handle.net/11336/129368 | |
dc.identifier | 1573-4935 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4372310 | |
dc.description.abstract | Protein S-acylation is a reversible post-translational modification involving the addition of fatty acids to cysteines and is catalyzed by transmembrane protein acyltransferases (PATs) mainly expressed at the Golgi complex. In case of soluble proteins, S-acylation confers stable membrane attachment. Myristoylation or farnesylation of many soluble proteins constitutes the initial transient membrane adsorption step prior to S-acylation. However, some S-acylated soluble proteins, such as the neuronal growth-associated protein Growth-associated protein-43 (GAP-43), lack the hydrophobic modifications required for this initial membrane interaction. The signals for GAP-43 S-acylation are confined to the first 13 amino acids, including the S-acylatable cysteines 3 and 4 embedded in a hydrophobic region, followed by a cluster of basic amino acids. We found that mutation of critical basic amino acids drastically reduced membrane interaction and hence S-acylation of GAP-43. Interestingly, acute depletion of phosphatidylinositol 4-phosphate (PtdIns4P) at the Golgi complex reduced GAP-43 membrane binding, highlighting a new, pivotal role for this anionic lipid and supporting the idea that basic amino acid residues are involved in the electrostatic interactions between GAP-43 and membranes of the Golgi complex where they are S-acylated. | |
dc.language | eng | |
dc.publisher | Portland Press | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://portlandpress.com/bioscirep/article/doi/10.1042/BSR20192911/221643/PtdIns4Pmediated-electrostatic-forces-influence | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1042/BSR20192911 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | S-ACYLATION | |
dc.subject | PALMITOYLATION | |
dc.subject | GAP-43 | |
dc.subject | PHOSPHOINOSITIDES | |
dc.title | PtdIns4P-mediated electrostatic forces influence S-acylation of peripheral proteins at the Golgi complex | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |