GRASP55

Last updated
GORASP2
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GORASP2 , GOLPH6, GRASP55, GRS2, p59, golgi reassembly stacking protein 2
External IDs OMIM: 608693 MGI: 2135962 HomoloGene: 9180 GeneCards: GORASP2
Orthologs
SpeciesHumanMouse
Entrez

26003

70231

Ensembl

ENSG00000115806

ENSMUSG00000014959

UniProt

Q9H8Y8

Q99JX3

RefSeq (mRNA)

NM_001201428
NM_015530

NM_027352

RefSeq (protein)

NP_001188357
NP_056345

NP_081628

Location (UCSC) Chr 2: 170.93 – 170.97 Mb Chr 2: 70.49 – 70.54 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Golgi reassembly-stacking protein of 55 k Da (GRASP55) also known as golgi reassembly-stacking protein 2 (GORASP2) is a protein that in humans is encoded by the GORASP2 gene. [5] [6] It was identified by its homology with GRASP65 and the protein's amino acid sequence was determined by analysis of a molecular clone of its complementary DNA. [5] The first (N-terminus) 212 amino acid residues of GRASP55 are highly homologous to those of GRASP65, but the remainder of the 454 amino acid residues are highly diverged from GRASP65. [5] The conserved region is known as the GRASP domain, and it is conserved among GRASPs of a wide variety of eukaryotes, but not plants. [6] [7] The C-terminus portion of the molecule is called the SPR domain (serine, proline-rich). [7] GRASP55 is more closely related to homologues in other species, suggesting that GRASP55 is ancestral to GRASP65. [7] GRASP55 is found associated with the medial and trans cisternae of the Golgi apparatus. [7]

Contents

Function

GRASP domain alignment of GRASP55 and the GRASP homologue of Cryptococcus neoformans CnGRASP55domainsc.jpg
GRASP domain alignment of GRASP55 and the GRASP homologue of Cryptococcus neoformans

GRASP55 is involved in establishing the structure of the Golgi apparatus. [7] [6] It is a peripheral membrane protein located on the Golgi cisterna, and it can bind to another GRASP55 located on an adjacent cisterna through the GRASP domain, thus linking the cisternae together through multiple protein–protein interactions. [7] [8]

GRASP55 is attached to the membrane in two ways; it is myristylated, which attaches it directly to the lipid bilayer; it is also bound indirectly by binding to golgin-45, which binds to a Rab protein, which itself is lipidated and thus anchored to the membrane. [7]

The structure of the Golgi is disrupted during mitosis, and phosphorylation of the SPR domains of GRASP55 and GRASP65 regulate that disruption, [9] [8] GRASP55 may also be involved in forming Golgi ribbons, but the evidence is mixed. [7] [9]

Other interactions

GRASP55 has been shown to interact with TGF alpha, [10] TMED2 [10] and GOLGA2. [5] [10] [11]

Related Research Articles

A cisterna are all of the membrane-bound sacs that could be found in both the Golgi apparatus and in the Endoplasmic Reticulum. Cisterna are an integral part of the packaging and modification processes of proteins occurring in the Golgi. It is the flattened sac on the branch of the Endoplasmic Reticulum and the curved sac on the branch of the Golgi apparatus. The proteins begin on the cis side of the Golgi and exit on the trans side. Throughout their journey in the cisterna, the proteins are packaged and are modified for transport throughout the cell. The number of cisterna in the Golgi stack is dependent on the organism and cell type. The structure, composition, and function of each of the cisternae may be different inside the Golgi stack. These different variations of Golgi cisternae are categorized into 3 groups; cis golgi network, medial, and trans Golgi network. The cis Golgi network is the first step in the cisternal structure of a protein being packaged, while the trans Golgi network is the last step in the cisternal structure when the vesicle is being transferred to either the lysosome, the cell surface or the secretory vesicle. The cisternae are shaped by the cytoskeleton of the cell through a lipid bilayer. Post-translational modifications such as glycosylation, phosphorylation and cleavage occur in the Golgi and as proteins travel through it, they go through the cisternae, which allows functional ion channels to be created due to these modifications. Each class of cisternae contains various enzymes used in protein modifications. These enzymes help the Golgi in glycosylation and phosphorylation of proteins, as well as mediate signal modifications to direct proteins to their final destination. Defects in the cisternal enzymes can cause congenital defects including some forms of muscular dystrophy, cystic fibrosis, cancer, and diabetes.

DCTN1 Protein-coding gene in the species Homo sapiens

Dynactin subunit 1 is a protein that in humans is encoded by the DCTN1 gene.

GOLGA2 Protein-coding gene in the species Homo sapiens

Golgin subfamily A member 2 is a protein that in humans is encoded by the GOLGA2 gene.

USO1 Protein-coding gene in the species Homo sapiens

General vesicular transport factor p115 is a protein that in humans is encoded by the USO1 gene.

DCTN2 Gene of the species Homo sapiens

Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene

RAB1A Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-1A is a protein that in humans is encoded by the RAB1A gene.

GRASP65 Protein-coding gene in the species Homo sapiens

Golgi reassembly-stacking protein of 65 kDa (GRASP65) also known as Golgi reassembly-stacking protein 1 (GORASP1) is a protein that in humans is encoded by the GORASP1 gene.

STX5 Protein-coding gene in the species Homo sapiens

Syntaxin-5 is a protein that in humans is encoded by the STX5 gene.

KIF20A

Kinesin-like protein KIF20A is a protein that in humans is encoded by the KIF20A gene.

TMED10

Transmembrane emp24 domain-containing protein 10 is a protein that in humans is encoded by the TMED10 gene.

GOLGA3

Golgin subfamily A member 3 is a protein that in humans is encoded by the GOLGA3 gene.

NSFL1C

NSFL1 cofactor p47 is a protein that in humans is encoded by the NSFL1C gene.

RAB2A Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-2A is a protein that in humans is encoded by the RAB2A gene.

BICD1 Protein-coding gene in the species Homo sapiens

Bicaudal D cargo adaptor 1 is a protein that in humans is encoded by the BICD1 gene.

GOLGA5 Protein-coding gene in the species Homo sapiens

Golgin subfamily A member 5 is a protein that in humans is encoded by the GOLGA5 gene.

BLZF1 Protein-coding gene in the species Homo sapiens

Golgin-45 is a protein that in humans is encoded by the BLZF1 gene.

KIFC1

Kinesin-like protein KIFC1 is a protein that in humans is encoded by the KIFC1 gene.

TMED2

Transmembrane emp24 domain-containing protein 2 is a protein that in humans is encoded by the TMED2 gene.

Golgi matrix

The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent and 150 mM NaCl. Treatment with a protease enzyme removed the matrix, which confirmed the importance of proteins for the matrix structure. Modern freeze etch electron microscopy (EM) clearly shows a mesh connecting Golgi cisternae and associated vesicles. Further support for the existence of a matrix comes from EM images showing that ribosomes are excluded from regions between and near Golgi cisternae.

Olwyn Byron is a British physicist who is Professor of Biophysics at the University of Glasgow and Chair of the British Biophysical Society. She was a member of the Physics of Life UK Network steering group who were awarded the 2020 Institute of Physics Rosalind Franklin Medal and Prize.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000115806 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000014959 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 3 4 Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA (September 1999). "GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system". The EMBO Journal. 18 (18): 4949–60. doi:10.1093/emboj/18.18.4949. PMC   1171566 . PMID   10487747.
  6. 1 2 3 "Entrez Gene: GORASP2 golgi reassembly stacking protein 2, 55kDa".
  7. 1 2 3 4 5 6 7 8 Zhang X, Wang Y (2015). "GRASPs in Golgi Structure and Function". Frontiers in Cell and Developmental Biology. 3: 84. doi: 10.3389/fcell.2015.00084 . PMC   4701983 . PMID   26779480.
  8. 1 2 Zhang, Xiaoyan; Wang, Yanzhuang (6 January 2016). "GRASPs in Golgi Structure and Function". Frontiers in Cell and Developmental Biology. 3: 84. doi: 10.3389/fcell.2015.00084 . PMC   4701983 . PMID   26779480.
  9. 1 2 Xiang Y, Wang Y (January 2010). "GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking". The Journal of Cell Biology. 188 (2): 237–51. doi:10.1083/jcb.200907132. PMC   2812519 . PMID   20083603.
  10. 1 2 3 Barr FA, Preisinger C, Kopajtich R, Körner R (December 2001). "Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus". The Journal of Cell Biology. 155 (6): 885–91. doi:10.1083/jcb.200108102. PMC   2150891 . PMID   11739402.
  11. ↑ Short B, Preisinger C, Körner R, Kopajtich R, Byron O, Barr FA (December 2001). "A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic". The Journal of Cell Biology. 155 (6): 877–83. doi:10.1083/jcb.200108079. PMC   2150909 . PMID   11739401.

Further reading

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