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  ESCRT recruitment by the S. cerevisiae inner nuclear membrane protein Heh1 is regulated by Hub1-mediated alternative splicing

Capella, M., Caballero, L. M., Pfander, B., Braun, S., & Jentsch, S. (2020). ESCRT recruitment by the S. cerevisiae inner nuclear membrane protein Heh1 is regulated by Hub1-mediated alternative splicing. Journal of Cell Science, 133(24): jcs250688. doi:10.1242/jcs.250688.

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 Creators:
Capella, Matías1, Author              
Caballero, Lucia Martin2, Author
Pfander, Boris3, Author              
Braun, Sigurd1, Author              
Jentsch, Stefan1, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
2International Max Planck Research School for Molecular and Cellular Life Sciences, 82152 Martinsried, Germany, ou_persistent22              
3Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565165              

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Free keywords: UBIQUITIN-LIKE PROTEIN; PORE COMPLEX; MOLECULAR-BASIS; KEY FEATURES; YEAST GENES; HUB1; LOCALIZATION; BINDING; ARCHITECTURE; EMERINCell Biology; ESCRT; LEM domain; Nuclear envelope surveillance; Nuclear pore complex; Splicing;
 Abstract: Misassembled nuclear pore complexes (NPCs) are removed by sealing off the surrounding nuclear envelope (NE), which is conducted by the endosomal sorting complexes required for transport (ESCRT) machinery. Recruitment of ESCRT proteins to the NE is mediated by the interaction between the ESCRT member Chm7 and the inner nuclear membrane protein Heh1, which belongs to the conserved LEM family. Increased ESCRT recruitment results in excessive membrane scission at damage sites but its regulation remains poorly understood. Here, we show that Hub1-mediated alternative splicing of HEH1 pre-mRNA, resulting in production of its shorter form Heh1-S, is critical for the integrity of the NE in Saccharomyces cerevisiae. ESCRT-III mutants lacking Hub1 or Heh1-S display severe growth defects and accumulate improperly assembled NPCs. This depends on the interaction of Chm7 with the conserved MSC domain, which is only present in the longer variant Heh1-L. Heh1 variants assemble into heterodimers, and we demonstrate that a unique splice segment in Heh1-S suppresses growth defects associated with the uncontrolled interaction between Heh1-L and Chm7. Together, our findings reveal that Hub1-mediated splicing generates Heh1-S to regulate ESCRT recruitment to the NE.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000608840900012
DOI: 10.1242/jcs.250688
 Degree: -

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Title: Journal of Cell Science
Source Genre: Journal
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Publ. Info: Cambridge, U.K. : Co. of Biologists
Pages: - Volume / Issue: 133 (24) Sequence Number: jcs250688 Start / End Page: - Identifier: ISSN: 0021-9533
CoNE: https://pure.mpg.de/cone/journals/resource/954925326678