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The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate.

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Shi, Y, Thomas, J O·1992·Molecular and Cellular Biology

Abstract

The 70-kDa heat shock protein hsp70 and its constitutively expressed cognate, hsc70, are abundant proteins implicated in a number of cellular processes. When a permeabilized cell system for examining the transport of proteins into the nucleus is depleted of hsc70 and hsp70, either by affinity chromatography on ATP-agarose or with antibodies against these proteins, nuclear transport activity is lost. Full activity is restored by the addition of HeLa proteins that bind to ATP-agarose. hsc70 and hsp70 are the active factors, since activity is also fully restored by the addition of either recombinant hsc70 or hsp70 which has been bacterially expressed and highly purified. The restoration of activity is saturable. The transport system requires other cytosolic factors as well, including at least one protein that is sensitive to inactivation by N-ethylmaleimide, but neither hsc70 nor hsp70 is the sensitive protein.

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Metadata

Authors
Shi, Y., & Thomas, J. O.
Venue
Molecular and Cellular Biology
Published
1992-05
Volume
12
Issue
5
Pages
2186-2192
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W2125778361
Cited by
343
References
0
FWCI
13.23
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. https://app.cochat.ai/papers/10.1128/mcb.12.5.2186
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Shi, Y., & Thomas, J. O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.12.5.2186

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.