Pannexin1(PANX1) is a channel protein which can be penetrated by many ions and molecules including ATP. It plays important roles in many physiological phenomena such as apoptosis and inflammation, and is considered as a potential therapeutic target. It can be activated by many different stimuli such as extracellular potassium, phosphorylation, protease cleavage, and intracellular calcium. Also its electrophysiological characteristic is complicated. Its characteristics as an ion channel need to be investigated in details. With the development of cryoelectron microscopy in recent years, the study of ion channels has reached a new stage, and the structure of PANX1 protein has been elucidated, including the activation mechanism, ion pathway and blocking mechanism of small molecule inhibitors. It is a heptamer rather than a hexamer as previously suspected. In addition to the main pore responsible for molecules like ATP, there are also side tunnels responsible for ion conducting. But still there are many problems remain unsolved. Cryo-EM structures didn’t show how C-tail exist in main pore of channel. This paper will introduce some basic characteristics of PANX1, and analyze the problems encountered in current studies, in order to put forward the key research objectives for future work.