Dephosphorylation of distinct sites on the 20 kDa myosin light chain by smooth muscle myosin phosphatase.
FEBS Lett
; 448(1): 101-4, 1999 Apr 01.
Article
en En
| MEDLINE
| ID: mdl-10217418
ABSTRACT
The dephosphorylation of the myosin light chain kinase and protein kinase C sites on the 20 kDa myosin light chain by myosin phosphatase was investigated. The myosin phosphatase holoenzyme and catalytic subunit, dephosphorylated Ser-19, Thr-18 and Thr-9, but not Ser-1/Ser-2. The role of noncatalytic subunits in myosin phosphatase was to activate the phosphatase activity. For Ser-19 and Thr-18, this was due to a decrease in Km and an increase in k(cat) and for Thr-9 to a decrease in Km. Thus, the distinction between the various sites is a property of the catalytic subunit.
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Banco de datos:
MEDLINE
Asunto principal:
Fosfoproteínas Fosfatasas
/
Cadenas Ligeras de Miosina
Límite:
Animals
/
Humans
Idioma:
En
Año:
1999
Tipo del documento:
Article