Cleaved KMT2A dimers translocate to the nucleus

Stable Identifier
R-HSA-9818576
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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The KMT2A (also known as MLL or MLL1) dimers, produced by the cleavage of KMT2A and subsequent dimerization of two cleaved fragments, translocate to the nucleus. While cleavage and dimerization are not needed for nuclear translocation, they are required for proper subnuclear localization of KMT2A (Hsieh, Ernst et al. 2003; Hsieh, Cheng and Korsmeyer 2003).

Hsieh, Ernst et al. 2003, and Hsieh, Cheng and Korsmeyer 2003: Recombinant and endogenous human TASP1 and KMT2A proteins were used, and experiments were performed in human embryonic kidney cell line HEK293.
Literature References
PubMed ID Title Journal Year
14636557 Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression

Hsieh, JJ, Cheng, EH, Korsmeyer, SJ

Cell 2003
12482972 Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization

Hsieh, JJ, Ernst, P, Erdjument-Bromage, H, Tempst, P, Korsmeyer, SJ

Mol Cell Biol 2003
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