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      Alternative splicing of the humanShakerK+channel β1 gene and functional expression of the β2 gene product

      , , , ,
      FEBS Letters
      Elsevier BV

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          Heteromultimeric K+ channels in terminal and juxtaparanodal regions of neurons.

          Voltage-gated potassium (K+) channels display a wide variety of conductances and gating properties in vivo. This diversity can be attributed not only to the presence of many K(+)-channel gene products, but also to the possibility that different K(+)-channel subunits co-assemble to form heteromultimeric channels in vivo. When expressed in Xenopus oocytes or transfected cells, K(+)-channel polypeptides assemble to form tetramers. Certain combinations of Shaker-like subunits have been shown to co-assemble, forming heteromultimeric channels with distinct properties. It is not known, however, whether K(+)-channel polypeptides form heteromultimeric channels in vivo. Here we describe the co-localization of two Shaker-like voltage-gated K(+)-channel proteins, mKv1.1 and mKv1.2, in the juxtaparanodal regions of nodes of Ranvier in myelinated axons, and in terminal fields of basket cells in mouse cerebellum. We also show that mKv1.1 and mKv1.2 can be coimmunoprecipitated with specific antibodies that recognize only one of them. These data indicate that the two polypeptides occur in subcellular regions where rapid membrane repolarization may be important and that they form heteromultimeric channels in vivo.
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            Auxiliary subunits of voltage-gated ion channels.

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              A characterization of the activating structural rearrangements in voltage-dependent Shaker K+ channels.

              In response to changes in membrane potential, voltage-dependent ion channel proteins undergo conformational rearrangements that lead to channel opening. These rearrangements move a net charge, measured as "gating current", across the membrane. Here we characterize the effects of the pharmacological blocker 4-aminopyridine on both the K+ and gating currents of wild-type and mutant Shaker K+ channels. Our results indicate that the activation of these channels involves two distinct types of structural rearrangement. In addition to independent Hodgkin and Huxley type rearrangements for each of the four subunits, which are responsible for most of the gating charge movement, Shaker channels interconvert between two quaternary conformations during activation. The transition between the two quaternary states moves about 10% of the total gating charge, and it is selectively blocked by 4-aminopyridine.
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                Author and article information

                Journal
                FEBS Letters
                Elsevier BV
                00145793
                August 14 1995
                August 14 1995
                : 370
                : 1-2
                : 32-36
                Article
                10.1016/0014-5793(95)00785-8
                04f30793-1426-46d5-b984-d572ed180393
                © 1995

                http://doi.wiley.com/10.1002/tdm_license_1.1

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