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Conference Paper

Selective Proteolysis By the Ubiquitin System

MPS-Authors
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Jentsch,  S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Heinlein,  R
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons284479

Jungmann,  J
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons276974

Reins,  H-A
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons289493

Schlenker,  S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Seufert,  W
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Sommer,  T
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Springer,  S       
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Jentsch, S., Heinlein, R., Jungmann, J., Reins, H.-A., Schlenker, S., Seufert, W., et al. (1996). Selective Proteolysis By the Ubiquitin System. In O. Resnekov, & A. Gabain (Eds.), Post-transcriptional Control of Gene Expression (pp. 187-191). Berlin, Germany: Springer.


Cite as: https://hdl.handle.net/21.11116/0000-000D-1AE7-2
Abstract
Intracellular protein levels are controlled by protein synthesis and degradation. A major proteolytic pathway of eukaryotes is ATP–dependent and requires the covalent attachment of ubiquitin, a small and highly conserved protein, to proteolytic substrates prior to degradation (for reviews see Finley & Chau 1991, Hershko & Ciechanover 1992, and Jentsch 1992a and b). This pathway is highly selective and mediates the elimination of abnormal proteins and controls the half–lives of some regulatory proteins. Known targets include transcriptional regulators (Hochstrasser et al. 1991), p53 (Scheffner et al. 1990), the Mos kinase (Nishizawa et al. 1992) and cyclins (Glotzer et al. 1991).