Published online August 27, 2007
doi:10.1083/jcb.200702120
The Journal of Cell Biology, Vol. 178, No. 5, 799-812
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Scarcelli et al.
The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes
John J. Scarcelli1,
Christine A. Hodge1, and
Charles N. Cole1,2
1 Department of Biochemistry and 2 Department of Genetics, Dartmouth Medical School, Hanover, NH 03755
Correspondence to Charles N. Cole: charles.cole{at}dartmouth.edu
Although the structure and function of components of the nuclear pore complex (NPC) have been the focus of many studies, relatively little is known about NPC biogenesis. In this study, we report that Apq12 is required for efficient NPC biogenesis in Saccharomyces cerevisiae. Apq12 is an integral membrane protein of the nuclear envelope (NE) and endoplasmic reticulum. Cells lacking Apq12 are cold sensitive for growth, and a subset of their nucleoporins (Nups), those that are primarily components of the cytoplasmic fibrils of the NPC, mislocalize to the cytoplasm. APQ12 deletion also causes defects in NE morphology. In the absence of Apq12, most NPCs appear to be associated with the inner but not the outer nuclear membrane. Low levels of benzyl alcohol, which increases membrane fluidity, prevented Nup mislocalization and restored the proper localization of Nups that had accumulated in cytoplasmic foci upon a shift to lower temperature. Thus, Apq12p connects nuclear pore biogenesis to the dynamics of the NE.
Abbreviations used in this paper: BA, benzyl alcohol; DiOC6, 3,3'- dihexyloxacarbocyanine iodide; IF, immunofluorescence; INM, inner nuclear membrane; NE, nuclear envelope; NPC, nuclear pore complex; Nup, nucleoporin; ONM, outer nuclear membrane; SPB, spindle pole body; UPR, unfolded protein response; UPRE, UPR element; WT, wild type.

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