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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
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]
Total Authors: 6
Affiliation:
[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
Total Affiliations: 3
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 194, p. 264-275, JAN 1 2022.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 16/16328-3 - Molecular dynamics simulations of proton dependent oligopeptide transporters
Grantee:Mariana Raquel Bunoro Batista
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 15/16812-0 - Multi-User Equipment approved in grant 2014/15546-1: SEC-MALS
Grantee:Richard Charles Garratt
Support Opportunities: Multi-user Equipment Program
FAPESP's process: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
Grantee:Antonio José da Costa Filho
Support Opportunities: Regular Research Grants
FAPESP's process: 12/20367-3 - Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans
Grantee:Antonio José da Costa Filho
Support Opportunities: Regular Research Grants
FAPESP's process: 18/13016-6 - Activation of Photosensitive Proteins with Radioluminescent Nanoparticles and X-Rays
Grantee:Mariana Chaves Micheletto
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 17/24669-8 - Unraveling the molecular bases of the early protein secretory pathway in humans using biophysical techniques
Grantee:Luis Felipe Santos Mendes
Support Opportunities: Scholarships in Brazil - Post-Doctoral