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Publication
Nuclear pore complex integrity requires Lnp1, a regulator of cortical
endoplasmic reticulum.
Authors Casey AK, Chen S, Novick P, Ferro-Novick S, Wente SR
Submitted By Submitted Externally on 11/3/2015
Status Published
Journal Molecular biology of the cell
Year 2015
Date Published 8/1/2015
Volume : Pages 26 : 2833 - 44
PubMed Reference 26041935
Abstract The nuclear envelope (NE) and endoplasmic reticulum (ER) are components of the
same contiguous membrane system and yet have distinct cellular functions.
Mounting evidence suggests roles for some ER proteins in the NE for proper
nuclear pore complex (NPC) structure and function. In this study, we identify a
NE role in Saccharomyces cerevisiae for Lnp1 and Sey1, proteins required for
proper cortical ER formation. Both lnp1? and sey1? mutants exhibit synthetic
genetic interactions with mutants in genes encoding key NPC structural
components. Both Lnp1 and Sey1 physically associate with other ER components
that have established NPC roles, including Rtn1, Yop1, Pom33, and Per33. Of
interest, lnp1? rtn1? mutants but not rtn1? sey1? mutants exhibit defects in NPC
distribution. Furthermore, the essential NPC assembly factor Ndc1 has altered
interactions in the absence of Sey1. Lnp1 dimerizes in vitro via its C-terminal
zinc finger motif, a property that is required for proper ER structure but not
NPC integrity. These findings suggest that Lnp1's role in NPC integrity is
separable from functions in the ER and is linked to Ndc1 and Rtn1 interactions.




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