Abstract:
:Pyruvate kinase M2 (M2-PK) controls the rate-limiting step at the end of the glycolytic pathway in normal proliferating and tumor cells. Other functions of M2-PK in addition to its role in glycolysis are little understood. The aim of this study was to identify new cellular interaction partners of M2-PK in order to discover novel links between M2-PK and cellular functions. Here we show that the SUMO-E3 ligase protein PIAS3 (inhibitor of activated STAT3) physically interacts with M2-PK and its isoenzyme M1-PK. Moreover, we demonstrate that endogenous SUMO-1-M2-PK conjugates exist in mammalian cells. Furthermore, we show that transient expression of PIAS3 but not the RING domain mutant PIAS3 (C299S, H301A) is consistent with nuclear localization of M2-PK and PIAS3 and M2-PK partially co-localize in the nucleus of these cells. This study suggests a link between PIAS3 and nuclear pyruvate kinase.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Spoden GA,Morandell D,Ehehalt D,Fiedler M,Jansen-Dürr P,Hermann M,Zwerschke Wdoi
10.1002/jcb.22125subject
Has Abstractpub_date
2009-05-15 00:00:00pages
293-302issue
2eissn
0730-2312issn
1097-4644journal_volume
107pub_type
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