Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family.
Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family.
复制标题
膜结合盘基网柄菌肌球蛋白重链激酶：蛋白激酶 C 家族的发育调节底物特异性成员。
DOI：
10.1073/pnas.89.13.5877
复制
发表时间：
1992
影响因子：
11.1
通讯作者：
Spudich,JA
中科院分区：
文献类型：
--
作者：
Ravid,S;Spudich,JA
利用该酶的特异性抗体，分离得到了Dictyostelium myosin heavy chain kinase （MHCK）基因的cDNA克隆。cDNA序列分析显示，Dictyostelium MHCK具有蛋白激酶C家族成员的所有结构域。MHCK的氨基末端区域含有富含半胱氨酸的基序，其内部重复存在于所有已知的蛋白激酶C物种中。该结构域位于与蛋白激酶催化结构域高度同源的序列之前。羧基末端区域包含一个由23个丝氨酸和苏氨酸残基组成的簇，可能代表Dictyostelium MHCK的自磷酸化结构域。这些结果以及先前的研究表明，该酶具有非常严格的底物特异性，通过自磷酸化反应每mol激酶含有大约20 mol磷酸盐，并且仅在发育过程中表达，这表明Dictyostelium MHCK是蛋白激酶C家族的独特成员，并暗示该激酶家族可能包括具有非常特定细胞功能的成员。可能比之前想象的还要复杂。
A cDNA clone corresponding to the Dictyostelium myosin heavy chain kinase (MHCK) gene was isolated using antibodies specific to the purified enzyme. Sequence analysis of the cDNA revealed that the Dictyostelium MHCK possesses all of the domains characteristic of members of the protein kinase C family. The amino-terminal region of the MHCK contains the cysteine-rich motif with an internal duplication that is present in all known protein kinase C species. This domain precedes sequences that are highly homologous to protein kinase catalytic domains. The carboxyl-terminal region contains a cluster of 23 serine and threonine residues that may represent the autophosphorylation domain of the Dictyostelium MHCK. These results, along with previous studies that indicate that this enzyme has very restrictive substrate specificity, incorporates approximately 20 mol of phosphate per mol of kinase through an autophosphorylation reaction, and is expressed only during development, suggest that the Dictyostelium MHCK is a distinct member of the protein kinase C family and imply that this kinase family, which may include members with very specific cellular functions, may be even more heterogeneous than previously thought.