PRK1在蛋白激酶C作用位点（丝氨酸152、丝氨酸156和丝氨酸163）使MARCKS磷酸化。
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163.
作者信息
Palmer R H, Schönwasser D C, Rahman D, Pappin D J, Herget T, Parker P J
机构信息
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, London, UK.
出版信息
FEBS Lett. 1996 Jan 15;378(3):281-5. doi: 10.1016/0014-5793(95)01454-3.
The 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) is a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified 'PKC' sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.
80kDa富含肉豆蔻酰化丙氨酸的蛋白激酶C底物（MARCKS）是蛋白激酶C（PKC）在体内的主要底物。在此我们报告，MARCKS是细胞提取物中脂质激活的PKC相关激酶（PRK1）的主要底物。此外，在体外PRK1被证明可在与PKC相同的位点磷酸化MARCKS。因此，在某些情况下，这些先前确定的“PKC”位点上MARCKS磷酸化的控制可能受PRK以及PKC介导的信号通路调控。本文讨论了MARCKS作为PKC激活标记和信号汇聚点的意义。
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