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The exquisite structural biophysics of the Golgi Reassembly and Stacking Proteins.

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Mendes LFS,Fontana NA,Reddy ST,Uversky VN,Costa-Filho AJ

doi

10.1016/j.ijbiomac.2020.08.203

subject

Has Abstract

pub_date

2020-12-01 00:00:00

pages

3632-3644

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)34301-4

journal_volume

164

pub_type

杂志文章,评审

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