Golgi reassembly-stacking protein 2

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

Golgi reassembly-stacking protein 2 ( GRS2) also known as Golgi reassembly-stacking protein of 55 kDa (GRASP55) is a protein that in humans is encoded by the GORASP2 gene.[5] It was identified by its homology with GORASP1 and the protein's amino acid sequence was determined by analysis of a molecular clone of its complementary DNA.[6] The first (N-terminus) 212 amino acid residues of GORASP2 are highly homologous to those of GORASP1, but the remainder of the 454 amino acid residues are highly diverged from GORASP1.[6] The conserved region is known as the GRASP domain, and it is conserved among GRASPs of a wide variety of eukaryotes, but not plants.[5][7] The C-terminus portion of the molecule is called the SPR domain (serine, proline-rich).[7] GORASP2 is more closely related to homologues in other species, suggesting that GORASP2 is ancestral to GORASP1.[7] GORASP2 is found associated with the medial and trans cisternae of the Golgi apparatus.[7]

Function

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GRASP domain alignment of GORASP2 and the GRASP homologue of Cryptococcus neoformans

GORASP2 is involved in establishing the structure of the Golgi apparatus.[7][5] It is a peripheral membrane protein located on the Golgi cisterna, and it can bind to another GRS2 located on an adjacent cisterna through the GRASP domain, thus linking the cisternae together through multiple protein–protein interactions.[7][8]

GRS2 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 GORASP2 and GORASP1 regulate that disruption,[9][8] GORASP2 may also be involved in forming Golgi ribbons, but the evidence is mixed.[7][9]

Other interactions

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GORASP2 has been shown to interact with TGF alpha,[10] TMED2[10] and GOLGA2.[6][10][11]

References

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  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 "Entrez Gene: GORASP2 golgi reassembly stacking protein 2, 55kDa".
  6. ^ a b c 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.
  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.
  8. ^ a b 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. ^ 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

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