PT  - JOURNAL ARTICLE
ED  - , 
TI  - Tied into Protein Degradation
AID  - 10.1126/stke.2000.14.tw8
DP  - 2000 Jan 11
TA  - Science's STKE
PG  - tw8--tw8
VI  - 2000
IP  - 14
4099  - http://stke.sciencemag.org/content/2000/14/tw8.short
4100  - http://stke.sciencemag.org/content/2000/14/tw8.full
SO  - Sci. STKE2000 Jan 11; 2000
AB  - 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]