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© The Rockefeller University Press, 0021-9525/1999//29 $5.00
The Journal of Cell Biology, Volume 146, Number 1, , 1999 29-44

Original Article

A Visual Screen of a Gfp-Fusion Library Identifies a New Type of Nuclear Envelope Membrane Protein



Melissa M. Rollsb, Pascal A. Steinb, Stephen S. Taylora, Edward Haa, Frank McKeona, and Tom A. Rapoportb

a Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115
b Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115
Department of Cell Biology, Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115.(617) 432-1190(617) 432-0637

tom_rapoport{at}hms.harvard.edu

The nuclear envelope (NE) is a distinct subdomain of the ER, but few membrane components have been described that are specific to it. We performed a visual screen in tissue culture cells to identify proteins targeted to the NE. This approach does not require assumptions about the nature of the association with the NE or the physical separation of NE and ER. We confirmed that screening a library of fusions to the green fluorescent protein can be used to identify proteins targeted to various subcompartments of mammalian cells, including the NE. With this approach, we identified a new NE membrane protein, named nurim. Nurim is a multispanning membrane protein without large hydrophilic domains that is very tightly associated with the nucleus. Unlike the known NE membrane proteins, it is neither associated with nuclear pores, nor targeted like lamin-associated membrane proteins. Thus, nurim is a new type of NE membrane protein that is localized to the NE by a distinct mechanism.

Key Words: nuclear envelope • nurim • green fluorescent protein • protein targeting • visual screen

© 1999 The Rockefeller University Press

1.used in this paper: CFP, cyan fluorescent protein; EST, expressed sequence tag; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; HO-2, heme oxygenase-2; LAP1 and -2, lamina-associated polypeptide 1 and -2; LBR, lamin B receptor; NE, nuclear envelope; TX-100, Triton X-100; VLP, visually localized protein; YFP, yellow fluorescent protein

P.A. Stein and M.M. Rolls contributed equally to this work.

S.S. Taylor's current address is School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.


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