Characterization of nuclear pore complex targeting domains in Pom152 in Saccharomyces cerevisiae.

Characterization of nuclear pore complex targeting domains in Pom152 in Saccharomyces cerevisiae.
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DOI:
10.1242/bio.057661
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发表时间:
2021-10-15
期刊:
影响因子:
2.4
通讯作者:
Belanger KD
Belanger KD
中科院分区:
生物学4区
文献类型:
--
作者:
Brown JT;Haraczy AJ;Wilhelm CM;Belanger KD

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Pom152 is a transmembrane protein within the nuclear pore complex (NPC) of fungi that is important for NPC assembly and structure. Pom152 is comprised of a short amino-terminal region that remains on the cytosolic side of the nuclear envelope (NE) and interacts with NPC proteins, a transmembrane domain, and a large, glycosylated carboxy-terminal domain within the NE lumen. Here we show that the N-terminal 200 amino acids of Pom152 that include only the amino-terminal and transmembrane regions are sufficient for localization to the NPC. Full-length, glycosylation-deficient, and truncated Pom152-GFP chimeras expressed in cells containing endogenous Pom152 localize to both NPCs and cortical endoplasmic reticulum (ER). Expression of Pom152-GFP fusions in pom152Δ cells results in detectable localization at only the NE by full-length and amino-terminal Pom152-GFP fusions, but continued retention at both the NE and ER for a chimera lacking just the carboxy-terminal 377 amino acids. Neither deletion of Pom152 nor its carboxy-terminal glycosylation sites altered the nuclear protein export rate of an Msn5/Kap142 protein cargo. These data narrow the Pom152 region sufficient for NPC localization and provide evidence that alterations in other domains may impact Pom152 targeting or affinity for the NPC. Summary: Pom152 is a transmembrane nucleoporin important for nuclear pore complex structure and synthesis. Here we further characterize Pom152, showing that the cytosolic and transmembrane domains are sufficient for NPC localization.
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