TY - JOUR
T1 - Assembly of mammalian voltage-gated potassium channels
T2 - Evidence for an important role of the first transmembrane segment
AU - Babila, Tamar
AU - Moscucci, Adriana
AU - Wang, Haiyan
AU - Weaver, Frances E.
AU - Koren, Gideon
N1 - Funding Information:
We are grateful to Dr. E. Neer and members of her laboratory for advice on the hydrodynamic experiments. We wish to thank Dr. S. C. Hebert and Mr. M. Lombardi for their assistance with the Xenopus oocyte experiments and for ROMK1 cDNA, Drs. E. Neer, T. Michel, B. Bean, and O. Strichartz for critical reading of the manuscript, and Dr. T. Smith for support and encouragement. This work was supported by a grant from the National Institutes of Health, H L46005, and a Grant in Aid from the American Heart Association to G. K.; T. B. is supported by a research fellowship award from the American Heart Association, Massachusetts affiliate. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC Section 1734 solely to indicate this fact.
PY - 1994/3
Y1 - 1994/3
N2 - Three different experimental approaches were used to establish that the first transmembrane segment (S1) is important for K+ channel assembly. First, hydrodynamic analyses of in vitro translated Kv1.1 N-terminal domain containing the S1 segment coassembles to form homo-tetrameric complexes, whereas deletion of the S1 segment abolishes coassembly. Second, coimmunoprecipitation experiments of cotranslated Kv1.1 and Kv1.5 truncated polypeptides show that the S1 segment is essential for coimmunoprecipitation. Third, dominant negative experiments in Xenopus oocytes confirm that over-expression of either the S1 segment or the N-terminal domain is sufficient for abolishing the expression of functional Kv1.1 and Kv1.5 K+ channels. These data indicate that S1 segment plays an important role in the coassembly of homo- and heterotetrameric K+ channels.
AB - Three different experimental approaches were used to establish that the first transmembrane segment (S1) is important for K+ channel assembly. First, hydrodynamic analyses of in vitro translated Kv1.1 N-terminal domain containing the S1 segment coassembles to form homo-tetrameric complexes, whereas deletion of the S1 segment abolishes coassembly. Second, coimmunoprecipitation experiments of cotranslated Kv1.1 and Kv1.5 truncated polypeptides show that the S1 segment is essential for coimmunoprecipitation. Third, dominant negative experiments in Xenopus oocytes confirm that over-expression of either the S1 segment or the N-terminal domain is sufficient for abolishing the expression of functional Kv1.1 and Kv1.5 K+ channels. These data indicate that S1 segment plays an important role in the coassembly of homo- and heterotetrameric K+ channels.
UR - https://www.scopus.com/pages/publications/0028264963
U2 - 10.1016/0896-6273(94)90217-8
DO - 10.1016/0896-6273(94)90217-8
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C2 - 8155323
AN - SCOPUS:0028264963
SN - 0896-6273
VL - 12
SP - 615
EP - 626
JO - Neuron
JF - Neuron
IS - 3
ER -