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Voltage-Gated K + Channel β Subunits: Expression and Distribution of Kvβ1 and Kvβ2 in Adult Rat Brain

Recent cloning of K + channel β subunits revealed that these cytoplasmic polypeptides can dramatically alter the kinetics of current inactivation and promote efficient glycosylation and surface expression of the channel-forming α subunits. Here, we examined the expression, distribution, and associat...

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Bibliographic Details
Published in:The Journal of neuroscience 1996-08, Vol.16 (16), p.4846-4860
Main Authors: Rhodes, Kenneth J., Monaghan, Michael M., Barrezueta, Nestor X., Nawoschik, Stanley, Bekele-Arcuri, Zewditu, Matos, Maria F., Nakahira, Kensuke, Schechter, Lee E., Trimmer, James S.
Format: Article
Language:English
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Summary:Recent cloning of K + channel β subunits revealed that these cytoplasmic polypeptides can dramatically alter the kinetics of current inactivation and promote efficient glycosylation and surface expression of the channel-forming α subunits. Here, we examined the expression, distribution, and association of two of these β subunits, Kvβ1 and Kvβ2, in adult rat brain. In situ hybridization using cRNA probes revealed that these β-subunit genes are heterogeneously expressed, with high densities of Kvβ1 mRNA in the striatum, CA1 subfield of the hippocampus, and cerebellar Purkinje cells, and high densities of Kvβ2 mRNA in the cerebral cortex, cerebellum, and brainstem. Immunohistochemical staining using subunit-specific monoclonal and affinity-purified polyclonal antibodies revealed that the Kvβ1 and Kvβ2 polypeptides frequently co-localize and are concentrated in neuronal perikarya, dendrites, and terminal fields, and in the juxtaparanodal region of myelinated axons. Immunoblot and reciprocal co-immunoprecipitation analyses indicated that Kvβ2 is the major β subunit present in rat brain membranes, and that most K + channel complexes containing Kvβ1 also contain Kvβ2. Taken together, these data suggest that Kvβ2 is a component of almost all K + channel complexes containing Kv1 α subunits, and that individual channels may contain two or more biochemically and functionally distinct β-subunit polypeptides.
ISSN:0270-6474
1529-2401
DOI:10.1523/JNEUROSCI.16-16-04846.1996