A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import [published erratum appears in J Cell Biol 1992 Jul;118(1):215]

doi:10.1083/jcb.117.3.473

This Article

	Full Text (PDF, 1857K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Stochaj, U.
	Articles by Silver, P. A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Stochaj, U.
	Articles by Silver, P. A.


Social Bookmarking

	What's this?

ARTICLES

A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import [published erratum appears in J Cell Biol 1992 Jul;118(1):215]

U Stochaj and PA Silver
Department of Molecular Biology, Princeton University, New Jersey 08544.

We have purified proteins of 70 kD from Drosophila, HeLa cells, and Z. mays that specifically bind nuclear localization sequences (NLSs). These proteins are recognized by antibodies raised against a previously identified NLS-binding protein (NBP) from the yeast S. cerevisiae. All NBPs are associated with nuclei and also present in the cytosol. NBPs are phosphorylated and phosphatase treatment abolished NLS binding. The requirement for NBPs in nuclear protein uptake is demonstrated in semipermeabilized Drosophila melanogaster tissue culture cells. Proper import of a fluorescent protein containing the large T antigen NLS requires cytosol and ATP. In the absence of cytosol and/or ATP, NLS- containing proteins are bound to cytosolic structures and the nuclear envelope. Addition of cytosol and ATP results in movement of this bound intermediate into the nucleus. Anti-NBP antibodies specifically inhibited the binding part of this import reaction. These results indicate that a phosphoprotein common to several eukaryotes acts as a receptor that recognizes NLSs before their uptake into the nucleus.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Ito, I., Fukazawa, J., Yoshida, M. (2007). Post-translational Methylation of High Mobility Group Box 1 (HMGB1) Causes Its Cytoplasmic Localization in Neutrophils. J. Biol. Chem. 282: 16336-16344 [Abstract] [Full Text]
Kodiha, M., Chu, A., Lazrak, O., Stochaj, U. (2005). Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70. Am. J. Physiol. Cell Physiol. 289: C1034-C1041 [Abstract] [Full Text]
Kasbohm, E. A., Guo, R., Yowell, C. W., Bagchi, G., Kelly, P., Arora, P., Casey, P. J., Daaka, Y. (2005). Androgen Receptor Activation by Gs Signaling in Prostate Cancer Cells. J. Biol. Chem. 280: 11583-11589 [Abstract] [Full Text]
Fang, X.-d., Chen, T., Tran, K., Parker, C. S. (2001). Developmental regulation of the heat shock response by nuclear transport factor karyopherin-{alpha}3. Development 128: 3349-3358 [Abstract] [Full Text]
Cserpan, I, Udvardy, A (1995). The mechanism of nuclear transport of natural or artificial transport substrates in digitonin-permeabilized cells. J. Cell Sci. 108: 1849-1861 [Abstract]
Vandromme, M, Carnac, G, Gauthier-Rouviere, C, Fesquet, D, Lamb, N, Fernandez, A (1994). Nuclear import of the myogenic factor MyoD requires cAMP-dependent protein kinase activity but not the direct phosphorylation of MyoD. J. Cell Sci. 107: 613-620 [Abstract]
Stochaj, U, Bossie, M., van Zee, K, Whalen, A., Silver, P. (1993). Analysis of conserved binding proteins for nuclear localization sequences. J. Cell Sci. 104: 89-95 [Abstract]