Abstract
The activity of a handful of transcription factors, such as mammalian NF-κB, Drosophila melanogaster Cubitus interruptus and yeast Spt23 and Mga2, are regulated through partial protein degradation by the proteasome. New data now show that the proteasome activates membrane-bound Spt23 and Mga2 by initiating their proteolysis at an internal site and then degrading the proteins bidirectionally toward both ends of the polypeptide chain, modifying our ideas on how the proteasome degrades targeted substrates.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 668-670 |
| Number of pages | 3 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 13 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 2006 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
Cite this
Where to start and when to stop. / Tian, Lin; Matouschek, Andreas.
In: Nature Structural and Molecular Biology, Vol. 13, No. 8, 08.2006, p. 668-670.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Where to start and when to stop
AU - Tian, Lin
AU - Matouschek, Andreas
PY - 2006/8
Y1 - 2006/8
N2 - The activity of a handful of transcription factors, such as mammalian NF-κB, Drosophila melanogaster Cubitus interruptus and yeast Spt23 and Mga2, are regulated through partial protein degradation by the proteasome. New data now show that the proteasome activates membrane-bound Spt23 and Mga2 by initiating their proteolysis at an internal site and then degrading the proteins bidirectionally toward both ends of the polypeptide chain, modifying our ideas on how the proteasome degrades targeted substrates.
AB - The activity of a handful of transcription factors, such as mammalian NF-κB, Drosophila melanogaster Cubitus interruptus and yeast Spt23 and Mga2, are regulated through partial protein degradation by the proteasome. New data now show that the proteasome activates membrane-bound Spt23 and Mga2 by initiating their proteolysis at an internal site and then degrading the proteins bidirectionally toward both ends of the polypeptide chain, modifying our ideas on how the proteasome degrades targeted substrates.
UR - http://www.scopus.com/inward/record.url?scp=33746821370&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33746821370&partnerID=8YFLogxK
U2 - 10.1038/nsmb0806-668
DO - 10.1038/nsmb0806-668
M3 - Article
C2 - 16886005
AN - SCOPUS:33746821370
VL - 13
SP - 668
EP - 670
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 8
ER -