GRASP55

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Golgi reassembly-stacking protein of 55 kDa (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]

GORASP2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGORASP2, GOLPH6, GRASP55, GRS2, p59, golgi reassembly stacking protein 2
External IDsOMIM: 608693; MGI: 2135962; HomoloGene: 9180; GeneCards: GORASP2; OMA:GORASP2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001201428
NM_015530

NM_027352

RefSeq (protein)

NP_001188357
NP_056345

NP_081628

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

Function

 
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]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115806Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000014959Ensembl, 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. ^ a b c d 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. ^ a b c "Entrez Gene: GORASP2 golgi reassembly stacking protein 2, 55kDa".
  7. ^ a b c d e f g h 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  8. ^ a b Zhang, Xiaoyan; Wang, Yanzhuang (6 January 2016). "GRASPs in Golgi Structure and Function". Frontiers in Cell and Developmental Biology. doi:10.3389/fcell.2015.00084.{{cite web}}: CS1 maint: unflagged free DOI (link)
  9. ^ a b 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. ^ a b c 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