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Research Article |
Departments of Medicine and of Anatomy and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA
* Author for correspondence (e-mail: hjw14{at}columbia.edu )
Accepted 9 January 2002
MAN1 is an integral protein of the inner nuclear membrane that shares the
LEM domain, a conserved globular domain of approximately 40 amino acids, with
lamina-associated polypeptide (LAP) 2 and emerin. Confocal immuofluorescence
microscopy studies of the intracellular targeting of truncated forms of MAN1
showed that the nucleoplasmic, N-terminal domain is necessary for inner
nuclear membrane retention. A protein containing the N-terminal domain with
the first transmembrane segment of MAN1 is retained in the inner nuclear
membrane, whereas the transmembrane segments with the C-terminal domain of
MAN1 is not targeted to the inner nuclear membrane. The N-terminal domain of
MAN1 is also sufficient for inner nuclear membrane targeting as it can target
a chimeric type II integral protein to this subcellular location. Deletion
mutants of the N-terminal of MAN1 are not efficiently retained in the inner
nuclear membrane. When the N-terminal domain of MAN1 is increased in size from
50 kDa to 100 kDa, the protein cannot reach the inner nuclear
membrane. Fluorescence recovery after photobleaching experiments of MAN1 fused
to green fluorescent protein show that the fusion protein is relatively
immobile in the nuclear envelope compared with the endoplasmic reticulum of
interphase cells, suggesting binding to a nuclear component. These results are
in agreement with the `diffusion-retention' model for targeting integral
proteins to the inner nuclear membrane.
Key words: Nuclear envelope, Inner nuclear membrane, LEM domain, Fluorescence recovery after photobleaching, ng, Membrane proteins, Muscular dystrophy
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