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Functional modulation of Kv4 channels by auxiliary KChIPs is of an extreme complexit-y. Recentco-crystal structure of Kv4 N-terminus/KChIP complex reveals a unique clam-ping mode of Kv4 andKChIP interaction with two-contact interfaces being involved inthe complex interaction.Theclamping mode has provided a structural framework in unde-rstanding the effects of KChIP1 on Kv4channel gating and possible surface expressio-n. Yet，many interesting questions still remain to beanswered. Does the second inte-rface affect the channel trafficking in any way besides promoting thetetrameric ass-embly? Since all KChIPs share the core regions but vary in their N-termini，do othe-r KChIPs form the structure similar to KChIP1? Can the clamping structure of KChIP1account forthe functional differences among other KChIPs（KChIP4a for instance) on K-v4 function?Understanding the molecular mechanism of Kv4 and KChIP interaction may lead to a betterunderstanding of the channel biology and function of native A-type K-v4 K+ currents. Because of therelevance of these findings to neuronal excitability,small molecules aimed at specific modulation ofKv4 and KChIP interaction may have th-erapeutic potentials for treatment of membraneexcitability-related disease conditio-ns.