Inhibition of nuclear protein import by a monoclonal antibody against a novel class of nuclear pore proteins

Pandey, Siyaram ; Karande, Anjali A. ; Mishra, Krishnaveni ; Parnaik, Veena K. (1994) Inhibition of nuclear protein import by a monoclonal antibody against a novel class of nuclear pore proteins Experimental Cell Research, 212 (2). pp. 243-254. ISSN 0014-4827

Full text not available from this repository.

Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00144...

Related URL: http://dx.doi.org/10.1006/excr.1994.1140

Abstract

Nuclear import of proteins is mediated by the nuclear pore complexes in the nuclear envelope and requires the presence of a nuclear localization signal (NLS) on the karyophilic protein. In this paper, we describe studies with a monoclonal antibody, Mab E2, which recognizes a class of nuclear pore proteins of 60-76 kDa with a common phosphorylated epitope on rat nuclear envelopes. The Mab E2-reactive proteins fractionated with the relatively insoluble pore complex-containing component of the envelope and gave a finely punctate pattern of nuclear staining in immunofluorescence assays. The antibody did not bind to any cytosolic proteins. Mab E2 inhibited the interaction of a simian virus 40 large T antigen NLS peptide with a specific 60-kDa NLS-binding protein from rat nuclear envelopes in photoaffinity labeling experiments. The antibody blocked the nuclear import of NLS--albumin conjugates in an in vitro nuclear transport assay with digitonin-permeabilized cells, but did not affect passive diffusion of a small non-nuclear protein, lysozyme, across the pore. Mab E2 may inhibit protein transport by directly interacting with the 60-kDa NLS-binding protein, thereby blocking signal-mediated nuclear import across the nuclear pore complex.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:34769
Deposited On:11 Apr 2011 14:00
Last Modified:11 Apr 2011 14:00

Repository Staff Only: item control page