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In Vitro Screening of Voltage-Gated Potassium Chimera Through Western Blot

AJAS · 2026

Shravya Bharathwaj · Southern California Academy of Sciences

Overview

Voltage-gated potassium channels (Kv channels) are a large and diverse family of membrane proteins that are essential in regulating the resting potential in cell membranes throughout the body. All mammalian Kv channels are made up of four α-subunits. Each subunit consists of six transmembrane domains (S1-S6), which connect the external and internal cell membrane. The S5 and S6 segments of the transmembrane domain form a pore that selectively allows potassium ions to pass through. Specifically, mammalian Kv1 α-subunits can also assemble with other Kv1 family channels (Kv1.1-Kv1.8) to form functional homo-/heterotetrameric channel complexes. Previous research has shown that the highly conserved pore domain sequences of Kv1 transmembrane regions contribute to distinct protein trafficking, which transports the protein to designated regions of the cell, as well as surface-expression behaviors; however, its exact mechanism is still unknown. Building upon this research, we found that by switching the P-S6 loops (involved in filtering ions) of Kv1.6 with Kv1.3 stills shows expression of this chimera protein. In addition, N-terminus and C-terminus deletions of Kv1.6 also resulted in expression despite these bigger modifications.

Competition history

  • AJAS 2026 Category not listed

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Source: AAAS Annual Meeting (Confex) / American Junior Academy of Science

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