Uncoupling substrate and activation functions of rotavirus NSP5: Phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation
Author | dc.contributor.author | Eichwald, Catherine | |
Author | dc.contributor.author | Jacob Ahumada, Germaine | es_CL |
Author | dc.contributor.author | Muszynski, Bartosz | es_CL |
Author | dc.contributor.author | Allende, Jorge E. | es_CL |
Author | dc.contributor.author | Burrone, Oscar R. | es_CL |
Admission date | dc.date.accessioned | 2007-05-04T19:01:54Z | |
Available date | dc.date.available | 2007-05-04T19:01:54Z | |
Publication date | dc.date.issued | 2004-11-16 | |
Cita de ítem | dc.identifier.citation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 101 (46): 16304-16309 NOV 16 2004 | en |
Identifier | dc.identifier.issn | 0027-8424 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/127121 | |
Abstract | dc.description.abstract | Rotavirus NSP5 is a nonstructural protein that localizes in viro-plasms of virus-infected cells. NSP5 interacts with NSP2 and undergoes a complex post-translational hyperphosphorylation, generating species with reduced PAGE mobility. Here we show that NSP5 operates as an autoregulator of its own phosphorylation as a consequence of two distinct activities of the protein: substrate and activator. We developed an in vivo hyperphosphorylation assay in which two NSP5 mutant constructs are cotransfected. One of them, fused to an 11-aa tag, served as substrate whereas the other was used to map NSP5 domains required for activation. The activation and substrate activity could be uncoupled, demonstrating a hyperphosphorylation process in trans between the activator and substratum. This process involved dimerization of the two components through the 18-aa C-terminal tail. Phosphorylation of Ser-67 within the SIDSAS motif (amino acids 63-67) was required to trigger hyperphosphorylation by promoting the activation function. We present evidence of casein kinase 1alpha being the protein kinase responsible for this key step as well as for the consecutive ones leading to NSP5 hyperphosphorylation. | en |
Lenguage | dc.language.iso | en | en |
Publisher | dc.publisher | NATL ACAD SCIENCES | en |
Keywords | dc.subject | DOUBLE-STRANDED-RNA | en |
Título | dc.title | Uncoupling substrate and activation functions of rotavirus NSP5: Phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation | en |
Document type | dc.type | Artículo de revista |
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