This is the current revision of this page, as edited by Citation bot(talk | contribs) at 21:41, 13 June 2022(Add: doi-access. | Use this bot. Report bugs. | Suggested by Headbomb | Linked from Wikipedia:WikiProject_Academic_Journals/Journals_cited_by_Wikipedia/Sandbox | #UCB_webform_linked 110/438). The present address (URL) is a permanent link to this version.
Revision as of 21:41, 13 June 2022 by Citation bot(talk | contribs)(Add: doi-access. | Use this bot. Report bugs. | Suggested by Headbomb | Linked from Wikipedia:WikiProject_Academic_Journals/Journals_cited_by_Wikipedia/Sandbox | #UCB_webform_linked 110/438)
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 GORASP2gene.[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]
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]
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID16964243. S2CID14294292.