Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The exquisite structural biophysics of the Golgi Reassembly and Stacking Proteins

Full text
Author(s):
Mendes, Luis F. S. [1] ; Fontana, Natalia A. [1] ; Reddy, S. Thirupathi [1] ; Uversky, Vladimir N. [2, 3, 4] ; Costa-Filho, Antonio J. [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Ribeirao Preto Sch Philosophy Sci & Literature, Phys Dept, Mol Biophys Lab, Ribeirao Preto - Brazil
[2] Univ S Florida, Morsani Coll Med, Dept Mol Med, Bruce B Downs Blvd, MDCO7, Tampa, FL 33612 - USA
[3] Univ S Florida, Morsani Coll Med, USF Hlth Byrd Alzheimers Res Inst, Bruce B Downs Blvd, MDCO7, Tampa, FL 33612 - USA
[4] Russian Acad Sci, Inst Biol Instrumentat, Fed Res Ctr, Pushchino Sci Ctr Biol Res, Pushchino 142290, Moscow Region - Russia
Total Affiliations: 4
Document type: Review article
Source: International Journal of Biological Macromolecules; v. 164, p. 3632-3644, DEC 1 2020.
Web of Science Citations: 0
Abstract

Golgi Reassembly and Stacking Proteins (GRASPs) were firstly described as crucial elements in determining the structure of the Golgi complex. However, data have been accumulating over the years showing GRASPs can participate in various cell processes beyond the Golgi maintenance, including cell adhesion and migration, autophagy and unconventional secretion of proteins. A comprehensive understanding of the GRASP functions requires deep mechanistic knowledge of its structure and dynamics, especially because of the unique structural plasticity observed for many members of this family coupled with their high promiscuity in mediating protein-protein interactions. Here, we critically review data regarding the structural biophysics of GRASPs in the quest for understanding the structural determinants of different functionalities. We dissect GRASP structure starting with the full-length protein down to its separate domains (PDZ1, PDZ2 and SPR) and outline some structural features common to all members of the GRASP family (such as the presence of many intrinsically disordered regions). Although the impact of those exquisite properties in vivo will still require further studies, it is possible, from our review, to pinpoint factors that must be considered in future interpretation of data regarding GRASP functions, thus bringing somewhat new perspectives to the field. (C) 2020 Elsevier B.V. All rights reserved. (AU)

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 type: Regular Research Grants
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 type: Regular Research Grants
FAPESP's process: 16/23863-2 - Molecular interactions of the Golgi Reassembly and Stacking Protein (GRASP) form Saccharomyces cerevisiae
Grantee:Natália Aparecida Fontana
Support type: Scholarships in Brazil - Doctorate (Direct)
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 type: Scholarships in Brazil - Post-Doctorate
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 type: Scholarships in Brazil - Post-Doctorate