Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 107, Issue 2, Pages 293-302Publisher
WILEY
DOI: 10.1002/jcb.22125
Keywords
GLYCOLYSIS; PYRUVATE KINASE; PKM2; SUMO-E3 LIGASE; PIAS3; SUMOYLATION
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Funding
- Austrian Science Funds (FWF Project) [P15383]
- Austrian Cancer Society, Tyrol
- Austrian Science Fund (FWF) [P15383] Funding Source: Austrian Science Fund (FWF)
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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. J. Cell. Biochem. 107: 293-302, 2009. (C) 2009 Wiley-Liss, Inc.
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