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The <scp>GRASP</scp> domain in golgi reassembly and stacking proteins: differences and similarities between lower and higher Eukaryotes
- Source :
- Web of Science, Repositório Institucional da UNESP, Universidade Estadual Paulista (UNESP), instacron:UNESP
- Publication Year :
- 2019
- Publisher :
- Wiley, 2019.
-
Abstract
- Made available in DSpace on 2020-12-10T19:35:32Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-09-01 Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) The Golgi complex is part of the endomembrane system and is responsible for receiving transport cargos from the endoplasmic reticulum and for sorting and targeting them to their final destination. To perform its function in higher eukaryotic cells, the Golgi needs to be correctly assembled as a flattened membrane sandwich kept together by a protein matrix. The precise mechanism controlling the Golgi cisternae assembly is not yet known, but it is widely accepted that the Golgi Reassembly and Stacking Protein (GRASP) is a main component of the Golgi protein matrix. Unlike mammalian cells, which have two GRASP genes, lower eukaryotes present only one gene and distinct Golgi cisternae assembly. In this study, we performed a set of biophysical studies to get insights on the structural properties of the GRASP domains (DGRASPs) from both human GRASP55 and GRASP65 and compare them with GRASP domains from lower eukaryotes (Saccharomyces cerevisiae and Cryptococcus neoformans). Our data suggest that both human DGRASPs are essentially different from each other and that DGRASP65 is more similar to the subgroup of DGRASPs from lower eukaryotes in terms of its biophysical properties. GRASP55 is present mainly in the Golgi medial and trans faces, which are absent in both fungi, while GRASP65 is located in the cis-Golgi. We suggest that the GRASP65 gene is more ancient and that its paralogue GRASP55 might have appeared later in evolution, together with the medial and trans Golgi faces in mammalians. Univ Sao Paulo, Fac Filosofia & Letras Ribeirao Preto, Dept Fis, Ribeirao Preto, Brazil Fundacao Oswaldo Cruz FIOCRUZ PE, Ctr Pesquisas Aggeu Magalhaes, Recife, PE, Brazil Univ Sao Paulo, Inst Fis, Dept Fis, Sao Paulo, Brazil Univ Estadual Paulista Julio Mesquita, IBILCE, Ctr Multiusuario Inovacao Biomol, Dept Fis, Sao Paulo, Brazil Univ Estadual Paulista Julio Mesquita, IBILCE, Ctr Multiusuario Inovacao Biomol, Dept Fis, Sao Paulo, Brazil CNPq: 303513/2016-0 FAPESP: 2016/23863-2 FAPESP: 2017/24669-8 FAPESP: 308380/2013-4 FAPESP: 2015/50366-7 FAPESP: 2012/20367-3 FAPESP: 2009/53989-4
- Subjects :
- 0301 basic medicine
spectroscopy
intrinsically disordered regions
Saccharomyces cerevisiae
Golgi reassembly
Matrix (biology)
Biochemistry
Evolution, Molecular
Fungal Proteins
03 medical and health sciences
symbols.namesake
0302 clinical medicine
Endomembrane system
Molecular Biology
Gene
golgi reassembly and stacking protein
biology
Endoplasmic reticulum
Golgi Matrix Proteins
Cell Biology
eukarya
Golgi apparatus
biology.organism_classification
Cell biology
030104 developmental biology
Structural Homology, Protein
030220 oncology & carcinogenesis
Cryptococcus neoformans
symbols
Golgi cisterna
GRASP domain
Function (biology)
Subjects
Details
- ISSN :
- 17424658 and 1742464X
- Volume :
- 286
- Database :
- OpenAIRE
- Journal :
- The FEBS Journal
- Accession number :
- edsair.doi.dedup.....a1afaf53bf6b705dbdcd3941d80edf5a
- Full Text :
- https://doi.org/10.1111/febs.14869