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Specification of Subunit Assembly by the Hydrophilic Amino-Terminal Domain of the Shaker Potassium Channel

Li, Min, Jan, Yuh Nung, Jan, Lily Yeh·1992·Science

Abstract

The functional heterogeneity of potassium channels in eukaryotic cells arises not only from the multiple potassium channel genes and splice variants but also from the combinatorial mixing of different potassium channel polypeptides to form heteromultimeric channels with distinct properties. One structural element that determines the compatibility of different potassium channel polypeptides in subunit assembly has now been localized to the hydrophilic amino-terminal domain. A Drosophila Shaker B (ShB) potassium channel truncated polypeptide that contains only the hydrophilic amino-terminal domain can form a homomultimer; the minimal requirement for the homophilic interaction has been localized to a fragment of 114 amino acids. Substitution of the amino-terminal domain of a distantly related mammalian potassium channel polypeptide (DRK1) with that of ShB permits the chimeric DRK1 polypeptide to coassemble with ShB.

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Metadata

Authors
Li, M., Jan, Y. N., & Jan, L. Y.
Venue
Science
Published
1992-08-28
Volume
257
Issue
5074
Pages
1225-1230
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1987313471
Cited by
455
References
0
FWCI
9.16
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Specification of Subunit Assembly by the Hydrophilic Amino-Terminal Domain of the Shaker Potassium Channel. https://app.cochat.ai/papers/10.1126/science.1519059
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Li, M., Jan, Y. N., & Jan, L. Y. (1992). Specification of Subunit Assembly by the Hydrophilic Amino-Terminal Domain of the Shaker Potassium Channel. Science. https://doi.org/10.1126/science.1519059

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