Deutsch
 
Benutzerhandbuch Datenschutzhinweis Impressum Kontakt
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

O-GlcNAcylation Prevents Aggregation of the Polycomb Group Repressor Polyhomeotic

MPG-Autoren
/persons/resource/persons77987

Gambetta,  Maria Cristina
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78423

Müller,  Jürg
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Gambetta, M. C., & Müller, J. (2014). O-GlcNAcylation Prevents Aggregation of the Polycomb Group Repressor Polyhomeotic. DEVELOPMENTAL CELL, 31(5), 629-639. doi:10.1016/j.devcel.2014.10.020.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-9098-1
Zusammenfassung
The glycosyltransferase Ogt adds O-linked N-Acetylglucosamine (O-GlcNAc) moieties to nuclear and cytosolic proteins. Drosophila embryos lacking Ogt protein arrest development with a remarkably specific Polycomb phenotype, arising from the failure to repress Polycomb target genes. The Polycomb protein Polyhomeotic (Ph), an Ogt substrate, forms large aggregates in the absence of O-GlcNAcylation both in vivo and in vitro. O-GlcNAcylation of a serine/threonine (SIT) stretch in Ph is critical to prevent nonproductive aggregation of both Drosophila and human Ph via their C-terminal sterile alpha motif (SAM) domains in vitro. Full Ph repressor activity in vivo requires both the SAM domain and O-GlcNAcylation of the SIT stretch. We demonstrate that Ph mutants lacking the SIT stretch reproduce the phenotype of ogt mutants, suggesting that the S/T stretch in Ph is the key Ogt substrate in Drosophila. We propose that O-GlcNAcylation is needed for Ph to form functional, ordered assemblies via its SAM domain.