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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.)

Biophysical characterization of intrinsically disordered human Golgi matrix protein GRASP65

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Author(s):
Reddy, S. Thirupathi [1] ; Uversky, Vladimir N. [2, 3] ; Costa-Filho, Antonio J. [1]
Total Authors: 3
Affiliation:
[1] Univ Sao Paulo, Ribeirao Preto Sch Philosophy Sci & Literature, Dept Phys, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ S Florida, Morsani Coll Med, USF Hlth Byrd Alzheimers Res Inst, Dept Mol Med, Tampa, FL 33620 - USA
[3] Russian Acad Sci, Inst Biol Instrumentat, Lab New Methods Biol, Fed Res Ctr, Pushchino Sci Ctr Biol Res, Pushchino, Moscow Region - Russia
Total Affiliations: 3
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 162, p. 1982-1993, NOV 1 2020.
Web of Science Citations: 0
Abstract

Golgi Reassembly and Stacking Proteins (GRASPs), including GRASP65/GRASP55, were firstly found as stacking factors of Golgi cisternae. Their involvement in other processes, such as unconventional protein secretion (UPS), have been demonstrated, suggesting GRASPs act as interaction hubs. However, structural details governing GRASP functions are not understood thoroughly. Here, we explored the structural features of human cis-Golgi GRASP65 in aqueous solution and compared them with those from trans-Golgi GRASP55. Besides their distinct Golgi localization, GRASP65/55 also seem to be selectively recruited to mitosis-related events or to UPS. Despite preserving the monomeric form in solution seen for GRASP55, as inferred from our SEC-MALS and DLS data, GRASP65 exhibited higher intrinsic disorder and susceptibility to denaturant than GRASP55 (disorder prediction, urea denaturation and circular dichroism data). Moreover, spectroscopic and microscopic studies showed for GRASP65 the same temperature-dependent amorphous aggregation and time-dependent amyloid fibrillation at 37 degrees C seen for GRASP55. In the latter case, however, GRASP65 presented a lower aggregation rate than GRASP55. The present and previous data evidenced that intrinsic disorder and formation of higher order oligomers, such as amyloid fibrils, are common features within GRASP family potentially impacting the protein's participation in cell processes. (C) 2020 Elsevier B.V. All rights reserved. (AU)

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: 17/12146-0 - Exploring the Biophysical Properties of Human Golgi Reassembly and Stacking Protein 55 in Solution and Its Interaction with Model Membranes
Grantee:Thirupathi Reddy Soudherpally
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: 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