Resurrecting Golgi proteins to grasp Golgi ribbon formation and self-association under stress

Autor(es)

Mendes, Luis F. S. ^[1] ; Batista, Mariana R. B. ^{[2, 1]} ; Kava, Emanuel ^[1] ; Bleicher, Lucas ^[3] ; Micheletto, Mariana C. ^[1] ; Costa-Filho, Antonio J. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Ribeirao Preto Sch Philosophy, Phys Dept, Mol Biophys Lab, Sao Paulo - Brazil

^[2] Univ Warwick, Sch Life Sci, Gibbet Hill Campus, Coventry, W Midlands - England

^[3] Univ Fed Minas Gerais, Inst Ciencias Biol, Belo Horizonte, MG - Brazil

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 194, p. 264-275, JAN 1 2022.
• Citações Web of Science: 0

Resumo

The Golgi complex is an essential organelle of the eukaryotic exocytic pathway. A subfamily of Golgi matrix proteins, called GRASPs, is central in stress-induced unconventional secretion, Golgi dynamics during mitosis/ apoptosis, and Golgi ribbon formation. The Golgi ribbon is vertebrate-specific and correlates with the appearance of two GRASP paralogues and two Golgins (GM130/Golgin45), which form specific GRASP-Golgin pairs. The molecular details of their appearance only in Metazoans are unknown. Moreover, despite new functionalities supported by GRASP paralogy, little is known about their structural and evolutionary differences. Here, we used ancestor sequence reconstruction and biophysical/biochemical approaches to assess the evolution of GRASPs structure/dynamics, fibrillation, and how they started anchoring their Golgin partners. Our data showed that a GRASP ancestor anchored Golgins before gorasp gene duplication in Metazoans. After gene duplication, variations within the GRASP binding pocket determined which paralogue would recruit which Golgin. These interactions are responsible for their specific Golgi location and Golgi ribbon appearance. We also suggest that GRASPs have a long-standing capacity to form supramolecular structures, affecting their participation in stress induced processes. (AU)

• Processo FAPESP: 16/16328-3 - Simulações de dinâmica molecular de transportadores de oligopeptídeos dependentes de prótons
• Beneficiário: Mariana Raquel Bunoro Batista
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 15/16812-0 - EMU concedido no processo 2014/15546-1: SEC-MALS
• Beneficiário: Richard Charles Garratt
• Modalidade de apoio: Auxílio à Pesquisa - Programa Equipamentos Multiusuários
• Processo FAPESP: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
• Beneficiário: Antonio José da Costa Filho
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/20367-3 - Estudos estruturais e funcionais da proteína de organização e compactação do Golgi (GRASP) de Cryptococcus neoformans
• Beneficiário: Antonio José da Costa Filho
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 18/13016-6 - Ativação de Proteínas Fotossensíveis com Nanopartículas Radioluminescentes e Raios-X
• Beneficiário: Mariana Chaves Micheletto
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 17/24669-8 - Desvendando as bases moleculares de processos iniciais da secreção de proteínas em humanos utilizando técnicas biofísicas
• Beneficiário: Luis Felipe Santos Mendes
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado