MassIVE MSV000099053

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ZAP triggers mRNA decay during the regulation of aberrant protein production

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Description

The endoplasmic reticulum (ER) is essential for the proper folding and processing of secretory and membrane proteins. These proteins are guided to the ER by signal peptides recognized by the signal recognition particle (SRP). When this process is impaired, cells rely on quality control mechanisms to prevent the accumulation of misfolded or mislocalized proteins. One such mechanism, known as regulation of aberrant protein production (RAPP), targets mRNAs encoding mutated signal peptides for degradation and also eliminates the corresponding aberrant proteins. Using a functional genetic screen, we identify the zinc finger antiviral protein (ZAP) as a key component of the RAPP pathway. Using proteomics and enhanced UV crosslinking and immunoprecipitation (eCLIP) experiments, we show that ZAP-S isoform associates with SRP components and facilitates degradation of aberrant mRNAs and proteins. ZAP exerts its role by recognizing faulty proteins early in their biogenesis and targeting them, along with their encoding mRNAs, for degradation. Loss of ZAP activates ER stress and the integrated stress response, highlighting its central role in safeguarding protein targeting and maintaining cellular homeostasis. [doi:10.25345/C5PZ5205H] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Signal recognition particle (SRP), Regulation of aberrant protein production (RAPP), Zinc finger antiviral protein (ZAP), mRNA degradation, ER stress ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Colin Wu, NCI, United States
Submitting User: ronholes7059
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