The carboxyl-terminal domains of MKP-1 and MKP-2 have inhibitory effects on their phosphatase activity.
In: Molecular and cellular biochemistry, Jg. 233 (2002-04-01), Heft 1-2, S. 107-17
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Zugriff:
Both the mitogen-activated protein kinase (MAPK) phosphatases MKP-1 and MKP-2 exert important feedback control of MAPK-mediated signaling events. The function of MKP-1 and MKP-2 is regulated via complex mechanisms, ranging from increased transcription of the MKP-1 and MKP-2 genes to post-translational catalytic activation of MKP-1 and MKP-2 proteins upon binding to their substrate MAPKs. In addition, MKP-1 stability increases upon ERK-dependent phosphorylation of two serine residues in its C-terminus. The C-terminal regions of MKP-1 and MKP-2, but not those of other MKPs, are homologous. To investigate the role of this domain, we have deleted the C-terminal tails from MKP-1 and MKP-2 and examined the effect of these deletions on their enzymatic activity. C-terminally truncated MKP-1 and MKP-2 exhibited, both in vivo and in vitro, substantially greater phosphatase activity towards their substrate MAPKs than did the full-length counterparts. However, C-terminal truncations did not significantly change either their substrate affinity, or their substrate-mediated catalytic activation. Basal phosphatase activity of the truncated proteins was also significantly higher than that of the wild-type counterparts. Collectively, these results suggest that the C-terminal domain may potentially play a role in the regulation of MKP-1 and MKP-2.
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The carboxyl-terminal domains of MKP-1 and MKP-2 have inhibitory effects on their phosphatase activity.
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Autor/in / Beteiligte Person: | Hutter, D ; Chen, P ; Li, J ; Barnes, J ; Liu, Y |
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Zeitschrift: | Molecular and cellular biochemistry, Jg. 233 (2002-04-01), Heft 1-2, S. 107-17 |
Veröffentlichung: | New York : Springer ; <i>Original Publication</i>: The Hague, Dr. W. Junk B. V. Publishers., 2002 |
Medientyp: | academicJournal |
ISSN: | 0300-8177 (print) |
DOI: | 10.1023/a:1015502226940 |
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