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首页> 外文期刊>Biochemistry >Characterization of mitogen-activated protein kinase (MAPK) dimers
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Characterization of mitogen-activated protein kinase (MAPK) dimers

机译：丝裂原活化蛋白激酶（MAPK）二聚体的表征

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Phosphorylated ERK2 has an increased capacity to form homodimers relative to unphosphorylated ERK2. We have characterized the nature of the ERK2 dimer and have mutated residues in the crystal dimer interface to examine the impact of dimerization on ERK2 activity. Analysis of the mutants by gel filtration indicates that at least five residues must be mutated simultaneously to produce an ERK2 mutant that is predominantly monomeric. Mutants, whether monomers or dimers, have specific protein kinase activities under fixed assay conditions that are roughly equivalent to wild-type ERK2. The ratio of dimers to monomers is increased as the salt concentration increases, consistent with a strong hydrophobic contribution to the energy of dimer formation. ERK2 dimerization also requires divalent cations. Sedimentation analysis indicates that the related c-Jun N-terminal kinase SAPK alpha I/JNK2 also forms dimers, but dimerization displays no dependence on phosphorylation; the unphosphorylated and phosphorylated forms of the kinase behave similarly, with low micromolar dimer dissociation constants.
机译：相对于未磷酸化的ERK2，磷酸化的ERK2具有更高的形成同二聚体的能力。我们已经表征了ERK2二聚体的性质，并在晶体二聚体界面中突变了残基，以检查二聚化对ERK2活性的影响。通过凝胶过滤对突变体的分析表明，必须同时突变至少五个残基才能产生主要为单体的ERK2突变体。突变体，无论是单体还是二聚体，在固定测定条件下均具有特定的蛋白激酶活性，该活性与野生型ERK2大致相当。随着盐浓度的增加，二聚体与单体的比例增加，这与对二聚体形成能量的强疏水作用相一致。 ERK2二聚化也需要二价阳离子。沉积分析表明，相关的c-Jun N端激酶SAPK alpha I / JNK2也形成二聚体，但二聚化不依赖于磷酸化。激酶的未磷酸化和磷酸化形式表现相似，但微摩尔二聚体的解离常数较低。

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