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PRMT-7/PRMT7 activates HLH-30/TFEB to guard plasma membrane integrity compromised by bacterial pore-forming toxins


ABSTRACT: Plasma membrane integrity (PMI) is essential for cellular homeostasis; thus, pore-forming toxins (PFTs) that disrupt host PMI significantly contribute to the virulence of various pathogens. However, how host cells protect PMI in response to PFT perforation in vivo remains obscure. Previously, we demonstrated that the HLH-30/TFEB-dependent intrinsic cellular defense (INCED) is elicited by PFT to maintain PMI in Caenorhabditis elegans intestinal epithelium. HLH-30/TFEB is a master transcription factor of autophagy, yet the molecular mechanism for the full activation of HLH-30/TFEB by PFT remains elusive. Here, we reveal that protein arginine methyltransferase-7 (PRMT-7) is indispensable to the nuclear transactivation of HLH-30. We demonstrated that PRMT-7 participates in the methylation of HLH-30 on its Rag complex binding domain to facilitate its nuclear localization. Moreover, we showed that PRMT7 is evolutionarily conserved to regulate TFEB cellular localization and repair plasma damage caused by PFT in human intestinal cells. Together, our observations not only unveil a novel PRMT7-dependent post-translational regulation of HLH-30/TFEB but also shed insight on the evolutionarily conserved mechanism of the INCED against PFT in metazoans.

ORGANISM(S): Caenorhabditis elegans

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PROVIDER: S-BSST1125 | biostudies-other |

REPOSITORIES: biostudies-other

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