Protein kinase CK1 interacts with and phosphorylates RanBPM in vitro

Sonja Wolff; Balbina García-Reyes; Doris Henne-Bruns; Joachim Bischof; Uwe Knippschild

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Protein kinase CK1 interacts with and phosphorylates RanBPM in vitro

机译：蛋白激酶CK1在体外与RanBPM相互作用并使其磷酸化

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Members of the casein kinase 1 (CK1) family of serine/threonine kinases are highly conserved from yeast to mammals and are involved in the regulation of various cellular processes. Specifically, the CK1 isoforms δ and ε have been shown to be involved in the regulation of proliferative processes, differentiation, circadian rhythm, as well as in the regulation of nuclear transport. In this report we show that CK1δ and ε interact with murine RanBPM in the yeast two-hybrid system (YTH) and that the putative CK1δ-interacting domains of RanBPM are located between aa 155-386 and aa 515-653. Furthermore, in mammalian cells CK1δ partially co-localizes with RanBPM and can be co-immunoprecipitated with RanBPM. In addition, CK1δ strongly phosphorylates RanBPM within aa 436-514 in vitro. The identification of the interacting and scaffolding protein RanBPM as a new substrate of CK1δ points towards a possible function for CK1δ in modulating RanBPM specific functions.

机译：酪氨酸/苏氨酸激酶的酪蛋白激酶1（CK1）家族成员从酵母到哺乳动物高度保守，并参与各种细胞过程的调控。具体而言，已显示CK1同工型δ和ε参与增殖过程，分化，昼夜节律的调节以及核转运的调节。在该报告中，我们显示了CK1δ和ε与酵母双杂交系统（YTH）中的鼠RanBPM相互作用，并且RanBPM的假定的与CK1δ相互作用的结构域位于aa 155-386和aa 515-653之间。此外，在哺乳动物细胞中，CK1δ与RanBPM部分共定位，并且可以与RanBPM共免疫沉淀。另外，CK1δ在体外在aa 436-514中强烈磷酸化RanBPM。相互作用和支架蛋白RanBPM作为CK1δ的新底物的鉴定指出了CK1δ在调节RanBPM特定功能中的可能功能。

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《Journal of Molecular Biochemistry》 |2015年第1期|共页
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Sonja Wolff; Balbina García-Reyes; Doris Henne-Bruns; Joachim Bischof; Uwe Knippschild;
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1. Protein p21(WAF1/CIP1) is phosphorylated by protein kinase CK2 in vitro and interacts with the amino terminal end of the CK2 beta subunit. [J] . Romero-Oliva F, Allende JE Journal of cellular biochemistry. . 2001,第3期

机译：蛋白p21（WAF1 / CIP1）在体外被蛋白激酶CK2磷酸化，并与CK2β亚基的氨基末端相互作用。
2. Kinase activity of casein kinase 1 delta (CK1 delta) is modulated by protein kinase C alpha (PKC alpha) by site-specific phosphorylation within the kinase domain of CK1 delta [J] . Meng Zhigang, Boehm Thomas, Xu Pengfei, Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics . 2019,第7a8期

机译：酪蛋白激酶1δ（CK1 delta）的激酶活性通过CK1 Delta的激酶结构域内的位点特异性磷酸化通过蛋白激酶Cα（PKCα）调节
3. Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. [J] . M T Diaz-Meco, M M Municio, P Sanchez, Molecular and Cellular Biology . 1996,第1期

机译：λ相互作用蛋白，一种新型蛋白，可与非典型蛋白激酶C同型λ/碘的锌指结构域特异性相互作用，并在体外和体内刺激其激酶活性。
4. PHOSPHORYLATED S6 KINASE AND S6 RIBOSOMAL PROTEIN ARE NOVEL BIOMARKERS OF ANTIBODY MEDIATED REJECTION IN HEART ALLOGRAFTS [C] . Fang Li, Jennifer Q. Zhang, David Gjertson, Clinical Histocompatibility Workshop. . 2010

机译：磷酸化的S6激酶和S6核糖体蛋白是心脏同种异体移植物中抗体介导的抗体的新型生物标志物
5. THE GLUCOSE TRANSPORTER IS A GLYCOPROTEIN OF M(R) 55,000 AND IS PROBABLY NOT PHOSPHORYLATED IN RESPONSE TO BIOLOGICAL ACTIVATORS OF TRANSPORT (HUMAN ERYTHROCYTE, PROTEIN KINASE C, MONOCLONAL ANTIBODIES). [D] . ALLARD, W. JEFFREY. 1986

机译：葡萄糖转运蛋白是M（R）55,000的糖蛋白，可能不被磷酸化以响应生物转运因子（人类红细胞，蛋白激酶C，单克隆抗体）。
6. RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation [O] . Ling Cheng, Sandra Lemmon, Vance Lemmon -1

机译：RanBPM是一种L1相互作用蛋白可调节L1介导的丝裂原激活的蛋白激酶激活
7. RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation [O] . Ling Cheng, Ra Lemmon, Vance Lemmon 2015

机译：RanBpm是一种L1相互作用蛋白，可调节L1介导的丝裂原活化蛋白激酶活化
8. Characterization of the Sites Phosphorylated on Tyrosine Hydroxylase by Ca(2+) and Phospholipid-Dependent Protein Kinase, Calmodulin-Dependent Multiprotein Kinase and Cyclic AMP-Dependent Protein Kinase [R] . Vulliet, P. R., Woodgett, J. R., Ferrari, S., 1985

机译：通过Ca（2+）和磷脂依赖性蛋白激酶，钙调蛋白依赖性多蛋白激酶和环amp依赖性蛋白激酶在酪氨酸羟化酶上磷酸化位点的表征

Protein kinase CK1 interacts with and phosphorylates RanBPM in vitro

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