Mass Spectrometry Reveals Protein Kinase CK2 High-Order Oligomerization via the Circular and Linear Assembly

作者：Seetoh Wei Guang^*; Chan Daniel Shiu Hin; Matak Vinkovic Dijana; Abell Chris^*

来源：ACS Chemical Biology, 2016, 11(6): 1511-1517.

DOI：10.1021/acschembio.6b00064

CK2 is an intrinsically active protein kinase that is crucial for cellular viability. However, conventional kinase regulatory mechanisms do not apply to CK2, and its mode of regulation remains elusive. Interestingly, CK2 is known to undergo reversible ionic-strength-dependent oligomerization. Furthermore, a regulatory mechanism based on autoinhibitory oligomerization has been postulated on the basis of the observation of circular trimeric oligomers and linear CK2 assemblies in various crystal structures. Here, we employ native mass spectrometry to monitor the assembly of oligomeric CK2 species in an ionic-strength-dependent manner. A subsequent. combination of ion mobility spectrometry mass spectrometry and hydrogen deuterium exchange mass spectrometry techniques was used to analyze the conformation of CK2 oligomers: Our findings support ionic-strength-dependent CK2 oligomerization, demonstrate the transient, nature of the alpha/beta interaction, and show that CK2 oligomerization proceeds via both the circular and linear assembly.

• 出版日期2016-6