The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate - PubMed (original) (raw)
The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate
Y Shi et al. Mol Cell Biol. 1992 May.
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.
Similar articles
- 70-kDa heat-shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro.
Okuno Y, Imamoto N, Yoneda Y. Okuno Y, et al. Exp Cell Res. 1993 May;206(1):134-42. doi: 10.1006/excr.1993.1129. Exp Cell Res. 1993. PMID: 8482354 - Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins.
Imamoto N, Matsuoka Y, Kurihara T, Kohno K, Miyagi M, Sakiyama F, Okada Y, Tsunasawa S, Yoneda Y. Imamoto N, et al. J Cell Biol. 1992 Dec;119(5):1047-61. doi: 10.1083/jcb.119.5.1047. J Cell Biol. 1992. PMID: 1332978 Free PMC article. - Role of heat shock cognate 70 protein in import of ornithine transcarbamylase precursor into mammalian mitochondria.
Terada K, Ohtsuka K, Imamoto N, Yoneda Y, Mori M. Terada K, et al. Mol Cell Biol. 1995 Jul;15(7):3708-13. doi: 10.1128/MCB.15.7.3708. Mol Cell Biol. 1995. PMID: 7791777 Free PMC article. - Aginactin, an agonist-regulated F-actin capping activity is associated with an Hsc70 in Dictyostelium.
Eddy RJ, Sauterer RA, Condeelis JS. Eddy RJ, et al. J Biol Chem. 1993 Nov 5;268(31):23267-74. J Biol Chem. 1993. PMID: 8226849 - The role of nucleoplasmin in chromatin assembly and disassembly.
Laskey RA, Mills AD, Philpott A, Leno GH, Dilworth SM, Dingwall C. Laskey RA, et al. Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):263-9; discussion 268-9. doi: 10.1098/rstb.1993.0024. Philos Trans R Soc Lond B Biol Sci. 1993. PMID: 8098530 Review.
Cited by
- Development of a UPLC-MRM-based targeted proteomic method to profile subcellular organelle marker proteins from human liver tissues.
Qiu X, Doyle LM, Wang MZ. Qiu X, et al. Sci Rep. 2022 Jun 29;12(1):10985. doi: 10.1038/s41598-022-15171-0. Sci Rep. 2022. PMID: 35768540 Free PMC article. - Exogenous H2 S prevents the nuclear translocation of PDC-E1 and inhibits vascular smooth muscle cell proliferation in the diabetic state.
Zhang L, Jiang X, Liu N, Li M, Kang J, Chen L, Tang J, Dong S, Lu F, Zhang W. Zhang L, et al. J Cell Mol Med. 2021 Sep;25(17):8201-8214. doi: 10.1111/jcmm.16688. Epub 2021 Aug 21. J Cell Mol Med. 2021. PMID: 34418283 Free PMC article. - Oxygen sensing, mitochondrial biology and experimental therapeutics for pulmonary hypertension and cancer.
Wu D, Dasgupta A, Read AD, Bentley RET, Motamed M, Chen KH, Al-Qazazi R, Mewburn JD, Dunham-Snary KJ, Alizadeh E, Tian L, Archer SL. Wu D, et al. Free Radic Biol Med. 2021 Jul;170:150-178. doi: 10.1016/j.freeradbiomed.2020.12.452. Epub 2021 Jan 12. Free Radic Biol Med. 2021. PMID: 33450375 Free PMC article. - The Multiple Roles and Therapeutic Potential of Molecular Chaperones in Prostate Cancer.
Hoter A, Rizk S, Naim HY. Hoter A, et al. Cancers (Basel). 2019 Aug 16;11(8):1194. doi: 10.3390/cancers11081194. Cancers (Basel). 2019. PMID: 31426412 Free PMC article. Review. - Nitric oxide contributes to protein homeostasis by S-nitrosylations of the chaperone HSPA8 and the ubiquitin ligase UBE2D.
Valek L, Heidler J, Scheving R, Wittig I, Tegeder I. Valek L, et al. Redox Biol. 2019 Jan;20:217-235. doi: 10.1016/j.redox.2018.10.002. Epub 2018 Oct 16. Redox Biol. 2019. PMID: 30368041 Free PMC article.
References
- Cell. 1991 Feb 8;64(3):489-97 - PubMed
- Cell. 1982 Sep;30(2):449-58 - PubMed
- J Cell Biol. 1991 Jul;114(1):169-83 - PubMed
- J Cell Biol. 1990 Nov;111(5 Pt 1):1775-83 - PubMed
- J Biol Chem. 1992 Jan 15;267(2):695-8 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous