dc.creator | Goitea, Victor Enrique | |
dc.creator | Hallak, Marta Elena | |
dc.date.accessioned | 2016-12-29T15:05:23Z | |
dc.date.accessioned | 2018-11-06T14:17:01Z | |
dc.date.available | 2016-12-29T15:05:23Z | |
dc.date.available | 2018-11-06T14:17:01Z | |
dc.date.created | 2016-12-29T15:05:23Z | |
dc.date.issued | 2015-06 | |
dc.identifier | Goitea, Victor Enrique; Hallak, Marta Elena; Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation; American Society For Biochemistry And Molecular Biology; Journal of Biological Chemistry; 290; 26; 6-2015; 16403-16414 | |
dc.identifier | 0021-9258 | |
dc.identifier | http://hdl.handle.net/11336/10587 | |
dc.identifier | 1083-351X | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1884787 | |
dc.description.abstract | Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT stability, we examined the metabolic fates and degradation mechanisms of cytoplasmic CRT and R-CRT in NIH 3T3 and CHO cells. Both CRT isoforms were found to be proteasomal substrates, but the half-life of R-CRT (2 h) was longer than that of cytoplasmic CRT (0.7 h). Arginylation was not required for proteasomal degradation of CRT, although R-CRT displays ubiquitin modification. A CRT mutant incapable of dimerization showed reduced metabolic stability of R-CRT, indicating that R-CRT dimerization may protect it from proteasomal degradation. Our findings, taken together, demonstrate a novel function of arginylation: increasing the half-life of CRT in cytoplasm. | |
dc.language | eng | |
dc.publisher | American Society For Biochemistry And Molecular Biology | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/290/26/16403 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http:/dx.doi.org/10.1074/jbc.M114.626127 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | ARGINYLATION | |
dc.subject | CALRETICULIN | |
dc.subject | PROTEASOME | |
dc.subject | PROTEIN DEGRADATION | |
dc.subject | PROTEIN TURNOVER | |
dc.subject | DIMER | |
dc.subject | POST-TRANSLATIONAL MODIFICATION | |
dc.subject | UBIQUITYLATION | |
dc.title | Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |