Evidence for an evolutionary relationship between Vmp1 and bacterial DedA proteins

VMP1 and DedA proteins are conserved families of transmembrane proteins in eukaryotes and prokaryotes respectively. Despite numerous reports involving these proteins in multiple cellular processes, their molecular function is still unknown. They share the domain of unknown function PF09335, suggesti...

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Detalhes bibliográficos
Autores: Tábara, Luis-Carlos, Vincent, Oliver, Escalante, Ricardo
Formato: artículo
Fecha de publicación:2019
País:España
Recursos:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/692322
Acesso em linha:http://hdl.handle.net/10486/692322
https://dx.doi.org/10.1387/ijdb.180312re
Access Level:acceso abierto
Palavra-chave:Autophagy
DedA
Ictyostelium
Lipid homeostasis
Vmp1
PF09335
SNARE-associated Golgi protein
Medicina
Descrição
Resumo:VMP1 and DedA proteins are conserved families of transmembrane proteins in eukaryotes and prokaryotes respectively. Despite numerous reports involving these proteins in multiple cellular processes, their molecular function is still unknown. They share the domain of unknown function PF09335, suggesting a possible functional relationship between these protein families. Here we show that VMP1 from different species contain two short motifs conserved in the bacterial DedA proteins and the yeast protein Tvp38. The hallmark of one of these motifs is a glycine residue previously shown to be strictly conserved in all the DedA proteins. Substitution of this residue to leucine, glutamate or arginine in Dictyostelium Vmp1 inactivates the protein, as shown by the inability of the mutants to rescue the phenotypes associated with the lack of Vmp1 including development and lipid homeostasis. This is the first experimental approach that supports an evolutionary relationship between Vmp1 and DedA proteins and highlights the importance of the conserved glycine residue in the PF09335 domain