Domain 3a mutation of VPS33A suppresses larval arrest phenotype in the loss of VPS45 in Caenorhabditis elegans

The Sec1/Munc18 (SM) protein VPS45 is a key regulator of SNARE-mediated membrane fusion in endosomal trafficking, but its precise role remains unknown. To understand the function of VPS45 , we performed a genetic suppressor screen in . We found that the temperature-sensitive lethality caused by the...

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Bibliographic Details
Published in:microPublication biology 2024, Vol.2024
Main Authors: Gengyo-Ando, Keiko, Kumagai, Masahiko, Ando, Hideki, Nakai, Junichi
Format: Article
Language:English
Online Access:Get full text
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Summary:The Sec1/Munc18 (SM) protein VPS45 is a key regulator of SNARE-mediated membrane fusion in endosomal trafficking, but its precise role remains unknown. To understand the function of VPS45 , we performed a genetic suppressor screen in . We found that the temperature-sensitive lethality caused by the loss of VPS-45 can be suppressed by a mutation in another SM protein, VPS33A. The VPS33A M376I mutation is located in domain 3a, which is predicted to be essential for SNARE complex assembly. These results highlight the functional importance of domain 3a in endosomal SM proteins and its role in specific membrane fusion.
ISSN:2578-9430
DOI:10.17912/micropub.biology.001155