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Nurminsky, D.I. et al.

Nurminsky, Nurminskaya, Benevolenskaya, Shevelyov, Hartl, Gvozdev,

Cytoplasmic dynein intermediate-chain isoforms with different targeting properties created by tissue-specific alternative splicing.

The intermediate chains (ICs) are the subunits of the cytoplasmic dynein that provide binding of the complex to cargo organelles through interaction of their N termini with dynactin. We present evidence that in Drosophila, the IC subunits are represented by at least 10 structural isoforms, created by the alternative splicing of transcripts from a unique Cdic gene. The splicing pattern is tissue specific. A constitutive set of four IC isoforms is expressed in all tissues tested; in addition, tissue-specific isoforms are found in the ovaries and nervous tissue. The structural variations between isoforms are limited to the N terminus of the IC molecule, where the interaction with dynactin takes place. This suggests differences in the dynactin- mediated organelle binding by IC isoforms. Accordingly, when transiently expressed in Drosophila Schneider-3 cells, the IC isoforms differ in their intracellular targeting properties from each other. A mechanism is proposed for the regulation of dynein binding to organelles through the changes in the content of the IC isoform pool.[1]

References

Cytoplasmic dynein intermediate-chain isoforms with different targeting properties created by tissue-specific alternative splicing. Nurminsky, D.I., Nurminskaya, M.V., Benevolenskaya, E.V., Shevelyov, Y.Y., Hartl, D.L., Gvozdev, V.A. Mol. Cell. Biol. (1998) [Pubmed]

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