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A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin

  1. Author:
    Chen, Y. W.
    Yu, P.
    Lu, D.
    Tagle, D. A.
    Cai, T.

  2. Author Address

    Georgetown Univ, Dept Physiol, Med Ctr, Washington, DC 20016 USA. Georgetown Univ, Dept Physiol, Med Ctr, Washington, DC 20016 USA. Fujing Med Univ, Fujian, Peoples R China. NCI, Struct Biophys Lab, Frederick, MD 21702 USA. Vet Affairs Med Ctr, Washington, DC 20016 USA. NHGRI, Genet & Mol Biol Branch, NIH, Bethesda, MD 20892 USA. NIDCR, Expt Med Sect, OIIB, NIH, Bethesda, MD 20892 USA. Chen YW Georgetown Univ, Dept Physiol, Med Ctr, Washington, DC 20016 USA.
    1. Year: 2001
  2. Journal: Journal of Molecular Neuroscience
    1. 17
    2. 1
    3. Pages: 59-70
  4. Type of Article: Article
  1. Abstract:

    We report the identification of a full-length novel beta - spectrin II gene (beta SpII Sigma2) in human brain. The beta SpII Sigma2 gene has 32 exons encoding an actin-binding domain, followed by 17-spectrin repeats, and a short COOH-terminal regulatory region that lacks the Pleckstrin homology (PH) domain. Pair-wise sequence analysis showed an additional 36 and 28 amino acids located at the NH2 and COOH-terminal regions of beta SpII Sigma2, respectively. Northern-blot analysis showed an abundant expression of beta SpII Sigma2 transcripts in brain, lung, and kidney. Western-blot analysis confirmed the predicted similar to 225 kD molecular size of beta SpII Sigma2 protein in these same tissues. In brain, immunofluorescent staining revealed that beta SPII Sigma2 was enriched in cerebellar neurons, with specific enrichment in Purkinje cell bodies, but not in dendrites. Of considerable interest, neurofibromatosis type 2 (NF2) gene product schwannomin was found to co-immunoprecipitate with beta SpII Sigma2 in cultured Purkinje cells. These results suggest that beta SpII Sigma2 may play an important role in the assembly of the specialized plasma membrane domain of Purkinje neurons and that schwannomin may be involved in actin-cytoskeleton organization by interacting with beta SpII Sigma2.

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