Abstract：
:In mammals, the Golgi apparatus is the central hub for intracellular trafficking, sorting and post-translational modifications of proteins and lipids. Golgi reassembly and stacking proteins (GRASPs) are somehow involved in Golgi stacking, which is relevant for its proper function, and also in unconventional protein secretion. However, the structural details on how GRASPs accomplish those tasks are still elusive. Here, we have explored the biochemical and biophysical properties of human full-length GRASP55 in solution. Sequence-based analyses and circular dichroism spectroscopy suggest that GRASP55 presents multiple intrinsically disordered sites, although keeping considerable contents of regular secondary structure. Size exclusion chromatography and multiple-angle light scattering show that GRASP55 are monomers in solution. Urea denaturation of GRASP55 suggests the transition to the unfolded state is a cooperative process. Differential scanning calorimetry analysis displays two endothermic transitions for GRASP55, indicating the existence of an intermediate state prior to unfolding. Thioflavin T fluorescence suggests GRASP55 intermediate can be aggregates/fibrils. Transmission electron microscopy and fluorescence lifetime imaging microscopy prove GRASP55 forms large amorphous aggregates but not amyloid-like fibrils in the intermediate state. These results could be helpful in discussing the proper function of human GRASP55 in the Golgi organization as well as unconventional secretion of proteins.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Reddy ST,Mendes LFS,Fontana NA,Costa-Filho AJdoi
10.1016/j.ijbiomac.2019.05.089subject
Has Abstractpub_date
2019-08-15 00:00:00pages
481-489eissn
0141-8130issn
1879-0003pii
S0141-8130(19)32378-5journal_volume
135pub_type
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