Major nucleolar proteins shuttle between nucleus and cytoplasm

doi:10.1016/0092-8674(89)90241-9

Cell

Volume 56, Issue 3, 10 February 1989, Pages 379-390

https://doi.org/10.1016/0092-8674(89)90241-9 Get rights and content

Abstract

Nucleolin is a 92 kd nucleolar protein implicated in regulating polymerase I transcription and binding of preribosomal RNA. Another abundant nucleolar protein of 38 kd ( $B23 No38$ ) is thought to be involved in intranuclear packaging of preribosomal particles. Although both proteins have previously been detected only in nuclei, we conclude that they shuttle constantly between nucleus and cytoplasm. This conclusion is based on monitoring the equilibration of these proteins between nuclei present in interspecies heterokaryons, and on observing the antigen-mediated nuclear accumulation of cytoplasmically injected antibodies. Our unexpected results suggest a role for these major nucleolar proteins in the nucleocytoplasmic transport of ribosomal components. Moreover, they suggest that transient exposure of shuttling proteins to the cytoplasm may provide a mechanism for cytoplasmic regulation of nuclear activities.

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Cell

ArticleMajor nucleolar proteins shuttle between nucleus and cytoplasm

Abstract

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Antibodies to a nucleolar protein are localized in the nucleolus after red blood cell-mediated microinjection

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Article
Major nucleolar proteins shuttle between nucleus and cytoplasm