Stress-induzierte posttranslationale Modifikationen des Y-box Proteins-1 (YB-1) beinhalten Acetylierung und Phosphorylierung

YB-1 is a member of the cold-shock domain protein superfamily. It performs a wide variety of cellular functions, including transcriptional and translational regulation, DNA repair, drug resistence and stress responses to extracellular signals. We demonstate increasing levels of acetylated endogenous YB-1 protein after cellular stress like heat shock treatment, uv-irradiation and stimulation with the cytokine Interferon-gamma. After the maximum of cellular stress YB-1 protein is prefentially localized in the nucleus. We also observed increasing levels of modificated YB-1 protein by phosphorylation. We demonstrate an interaction between endogenous YB-1 protein and acetyltransferase CBP as well as the histondeacetylases HDAC-1 and Sirt1. After stimulation with PDGF-BB a protein complex with a molecular weight of 52kDa was observed. By MALDI-TOF analysis YB-1 protein was detected. We suppose two other cleavage site in the C-terminus of YB-1 protein and previous to aminoacid 82.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2008

Author dc:creator

• Knott, Hanna

Contributors dc:contributor

• Mertens, Peter René

• info:eu-repo/classification/ddc/610
• Acetylierung
• Phosphorylierung
• Histon-Deacetylase
• Cap-Bindungsprotein
• Medizin
• Posttranslationale Modifikation
• zellulärer Stress
• Acetyltransferasen
• Histondeacetylasen
• YB-1
• acetylation
• phosphorylation
• cellular stress
• acetyltransferases
• HDAC
• posttranslational modification

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-112815%22

OAI record oai:identifier

https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A50264