1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak

Abstract

Ahnak is a ~ 700 kDa polypeptide that was originally identified as a tumour-related nuclear phosphoprotein, but later recognized to play a variety of diverse physiological roles related to cell architecture and migration. A critical function of Ahnak is modulation of Ca signaling in cardiomyocytes by interacting with the β subunit of the L-type Ca channel (Ca1.2). Previous studies have identified the C-terminal region of Ahnak, designated as P3 and P4 domains, as a key mediator of its functional activity. We report here the nearly complete H,C and N backbone NMR chemical shift assignments of the 11 kDa C-terminal P4 domain of Ahnak. This study lays the foundations for future investigations of functional dynamics, structure determination and interaction site mapping of the Ca1.2-Ahnak complex.

AHNAKs roles in physiology and malignant tumors

“…AHNAK can be involved in a wide range of biological processes ( Figure 1 ). It has been recently reported that AHNAK plays a critical role in the regulation of calcium channels, blood-brain barrier formation, embryonic development, lipid metabolism, membrane repair, inflammatory responses and other processes ( 11 ). However, compared to AHNAK, the function of AHNAK2 is still relatively poorly studied and its biological function is not well defined.…”