Proximity labeling proteomics reveals critical regulators for inner nuclear membrane protein degradation in plants

Aobo Huang, Yu Tang, Xuetao Shi, Min Jia, Jinheng Zhu, Xiaohan Yan, Huiqin Chen and Yangnan Gu ()
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Aobo Huang: Tsinghua University
Yu Tang: University of California
Xuetao Shi: Tsinghua University
Min Jia: University of California
Jinheng Zhu: Tsinghua University
Xiaohan Yan: Tsinghua University
Huiqin Chen: Tsinghua University
Yangnan Gu: University of California

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract The inner nuclear membrane (INM) selectively accumulates proteins that are essential for nuclear functions; however, overaccumulation of INM proteins results in a range of rare genetic disorders. So far, little is known about how defective, mislocalized, or abnormally accumulated membrane proteins are actively removed from the INM, especially in plants and animals. Here, via analysis of a proximity-labeling proteomic profile of INM-associated proteins in Arabidopsis, we identify critical components for an INM protein degradation pathway. We show that this pathway relies on the CDC48 complex for INM protein extraction and 26S proteasome for subsequent protein degradation. Moreover, we show that CDC48 at the INM may be regulated by a subgroup of PUX proteins, which determine the substrate specificity or affect the ATPase activity of CDC48. These PUX proteins specifically associate with the nucleoskeleton underneath the INM and physically interact with CDC48 proteins to negatively regulate INM protein degradation in plants.

Date: 2020
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DOI: 10.1038/s41467-020-16744-1

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