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 Macromoljournal_title
International journal of biological macromoleculesauthors
Mendes LFS,Fontana NA,Reddy ST,Uversky VN,Costa-Filho AJdoi
10.1016/j.ijbiomac.2020.08.203subject
Has Abstractpub_date
2020-12-01 00:00:00pages
3632-3644eissn
0141-8130issn
1879-0003pii
S0141-8130(20)34301-4journal_volume
164pub_type
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