Phosphorylation of the minimal inhibitory region at the C-terminus of caldesmon alters its structural and actin binding properties

Patchell, V.B.; Vorotnikov, A.V.; Gao, Y.; Low, D.G.; Evans, J.S.; Fattoum, A.; El-Mezgueldi, M.; Marston, S.B.; Levine, B.A.

Авторы: Patchell Valerie B., Vorotnikov Alexander V., Gao Yuan, Low Douglas G., Evans James S., Fattoum Abdellatif, El-Mezgueldi Mohammed, Marston Steven B., Levine Barry A.
Журнал: Biochimica et Biophysica Acta - General Subjects
Том: 1596
Номер: 1
Год издания: 2002
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 121
Последняя страница: 130
Аннотация: Caldesmon is an inhibitory protein believed to be involved in the regulation of thin filament activity in smooth muscles and is a major cytoplasmic substrate for MAP kinase. NMR spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon MAP kinase phosphorylation of Ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to F-actin. The structural basis for the altered interaction is identified from the observation that phosphorylation destabilises a turn segment linking the two actin binding sites and thereby results in the randomisation of their relative disposition. This modulatory influence of Ser-759 phosphorylation is not merely a function of the bulkiness of the covalent modification since the stability of the turn region is observed to be sensitive to the ionisation state of the phosphate group. The data are discussed in the context of the inhibitory association of the C-terminal domain of caldesmon with F-actin.
Добавил в систему: Воротников Александр Вячеславович

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Phosphorylation of the minimal inhibitory region at the C-terminus of caldesmon alters its structural and actin binding propertiesстатья

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