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Sci. STKE, 11 January 2000
Vol. 2000, Issue 14, p. tw8
[DOI: 10.1126/stke.2000.14.tw8]

EDITORS' CHOICE

Cell Biology Tied into Protein Degradation

The list of key signaling events that are regulated by controlled ubiquitin-dependent degradation of proteins continues to grow. Brondello et al. report that MAP kinase phosphatase-1 (MKP-1), which dephosphorylates and inactivates the p42 and p44 mitogen-activated protein (MAP) kinases, is degraded by the proteasome. The phosphatase itself is a target of the p42 MAPK and p44 MAPK enzymes that it inactivates. This phosphorylation of MKP-1 appears not to regulate its enzymatic activity, but rather to decrease its ubiquitin-dependent degradation. The MAP kinases also increase transcription of the gene encoding MKP-1, thus providing two signals that increase the abundance of MKP-1. Such regulation would appear to limit prolonged activation of the p42 and p44 MAP kinases.

Brondello, J-M., Pouysségur, J., and McKenzie, F.R. (1999) Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. Science 286: 2514-2517. [Abstract] [Full Text]

Citation: Tied into Protein Degradation. Sci. STKE 2000, tw8 (2000).


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