FIND ARTICLE

Volume: 
Issue: 
3
Date of issue: 

Glycosylation, consisting in incorporation of single N-acetylglucosamine residues attached by O-linkage to serine or threonine residues, is a common modification of nuclear proteins. Numerous chromatin and nuclear pore complex proteins as well as RNA polymerase II and some transcription factors are glycosylated in this unusual way. O-glycosylation of nuclear proteins has been postulated to play a role in nucleus-cytoplasmic transport, transcriptional regulation and regulation of protein phosphorylation level. In this paper data concerning enzymes engaged in O-glycosylation and deglycosylation of proteins, attachment sites of N-acetylglucosamine residues and known nuclear glycoproteins have been described.

Author of the article: 

The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email: mnowicki@ump.edu.pl

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