|
|
|
|
|
|
|
||
J. Cell Biol.,
Volume 143, Number 7, December 28, 1998 1801-1812
* Program in Molecular Medicine and Tpr is a 270-kD coiled-coil protein localized
to intranuclear filaments of the nuclear pore complex
(NPC). The mechanism by which Tpr contributes to the
structure and function of the nuclear pore is currently
unknown. To gain insight into Tpr function, we expressed the full-length protein and several subdomains
in mammalian cell lines and examined their effects on
nuclear pore function. Through this analysis, we identified an NH2-terminal domain that was sufficient for association with the nucleoplasmic aspect of the NPC. In
addition, we unexpectedly found that the acidic COOH
terminus was efficiently transported into the nuclear interior, an event that was apparently mediated by a putative nuclear localization sequence. Ectopic expression
of the full-length Tpr caused a dramatic accumulation
of poly(A)+ RNA within the nucleus. Similar results
were observed with domains that localized to the NPC
and the nuclear interior. In contrast, expression of
these proteins did not appear to affect nuclear import.
These data are consistent with a model in which Tpr is tethered to intranuclear filaments of the NPC by its
coiled coil domain leaving the acidic COOH terminus
free to interact with soluble transport factors and mediate export of macromolecules from the nucleus.
Department of Molecular Cell Biology, University of Massachusetts Medical School,
Worcester, Massachusetts 01605; and § Department of Cell Biology and Anatomy, University of Calgary, Calgary, Alberta,
Canada T2N 4N1
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
