Direct binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations

• DOI: 10.1083/jcb.202004222
• Publication Date: 2021-01-19T14:07:34Z
• Authors: David J. Thaller; Danqing Tong; Christopher J. Ma...; Nicholas R. Ader; Philip J. Mannino; Sapan Borah; Megan C. King; Barbara Ciani; C. Patrick Lusk
• Keywords: ESCRT; Nuclear pore; Nuclear membrane; Inner membrane

Mechanisms that control nuclear membrane remodeling are essential to maintain the integrity of nucleus but remain be fully defined. Here, we identify a phosphatidic acid (PA)–binding capacity in envelope (NE)–specific ESCRT, Chm7, budding yeast. Chm7’s interaction with PA-rich membranes is mediated through conserved hydrophobic stretch amino acids, which confers recruitment NE manner independent required for LAP2-emerin-MAN1 (LEM) domain protein Heh1 (LEM2). Consistent functional importance PA binding, mutation this region abrogates Chm7 and abolishes function context herniations form during defective pore complex (NPC) biogenesis. In fact, show sensor specifically accumulates within these herniations. We suggest local metabolism important ensuring productive its dysregulation may contribute pathologies associated NPC assembly.