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Journal Article

Taking a bite: proteasomal protein processing

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78542

Rape,  M.
Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78165

Jentsch,  S.
Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Rape, M., & Jentsch, S. (2002). Taking a bite: proteasomal protein processing. Nature Cell Biology, 4(5), E113-E116.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F4C-D
Abstract
The proteasome is a hollow cylindrical protease that contains active sites concealed within its central cavity. Proteasomes usually completely degrade substrates into small peptides, but in a few cases, degradation can yield biologically active protein fragments. Examples of this are the transcription factors NF-kappaB, Spt23p and Mga2p, which are generated from precursors by proteasomal processing. How distinct protein domains are spared from degradation remains a matter of debate. Here, we discuss several models and suggest a novel mechanism for proteasomal processing.