» Articles » PMID: 19727557

Localization of Golgi-resident Glycosyltransferases

Overview
Publisher Springer
Specialty Biology
Date 2009 Sep 4
PMID 19727557
Citations 71
Authors
Affiliations
Soon will be listed here.
Abstract

For many glycosyltransferases, the information that instructs Golgi localization is located within a relatively short sequence of amino acids in the N-termini of these proteins comprising: the cytoplasmic tail, the transmembrane spanning region, and the stem region (CTS). Also, one enzyme may be more reliant on a particular region in the CTS for its localization than another. The predominance of these integral membrane proteins in the Golgi has seen these enzymes become central players in the development of membrane trafficking models of transport within this organelle. It is now understood that the means by which the characteristic distributions of glycosyltransferases arise within the subcompartments of the Golgi is inextricably linked to the mechanisms that cells employ to direct the flow of proteins and lipids within this organelle.

Citing Articles

Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates.

Sumya F, Aragon-Ramirez W, Lupashin V bioRxiv. 2024; .

PMID: 39484492 PMC: 11527126. DOI: 10.1101/2024.10.25.620336.


The role of antibody glycosylation in autoimmune and alloimmune kidney diseases.

Beyze A, Larroque C, le Quintrec M Nat Rev Nephrol. 2024; 20(10):672-689.

PMID: 38961307 DOI: 10.1038/s41581-024-00850-0.


Glycoprofiling of proteins as prostate cancer biomarkers: A multinational population study.

Pinkeova A, Tomikova A, Bertokova A, Fabinyova E, Bartova R, Jane E PLoS One. 2024; 19(3):e0300430.

PMID: 38498504 PMC: 10947713. DOI: 10.1371/journal.pone.0300430.


Simulated digestions of free oligosaccharides and mucin-type O-glycans reveal a potential role for Clostridium perfringens.

McDonald A, Lisacek F Sci Rep. 2024; 14(1):1649.

PMID: 38238389 PMC: 10796942. DOI: 10.1038/s41598-023-51012-4.


Efficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells.

Liu W, Long Y, Bao Y, Li Y, Deng M, Yang X Acta Biochim Biophys Sin (Shanghai). 2023; 54(12):1841-1853.

PMID: 36789692 PMC: 10157534. DOI: 10.3724/abbs.2022184.


References
1.
Machamer C, Grim M, Esquela A, Chung S, Rolls M, Ryan K . Retention of a cis Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain. Mol Biol Cell. 1993; 4(7):695-704. PMC: 300979. DOI: 10.1091/mbc.4.7.695. View

2.
Shestakova A, Zolov S, Lupashin V . COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation. Traffic. 2006; 7(2):191-204. DOI: 10.1111/j.1600-0854.2005.00376.x. View

3.
de Graffenried C, Bertozzi C . The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus. Curr Opin Cell Biol. 2004; 16(4):356-63. DOI: 10.1016/j.ceb.2004.06.007. View

4.
Goto M . Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci Biotechnol Biochem. 2007; 71(6):1415-27. DOI: 10.1271/bbb.70080. View

5.
Becker B, Haggarty A, Romero P, Poon T, HERSCOVICS A . The transmembrane domain of murine alpha-mannosidase IB is a major determinant of Golgi localization. Eur J Cell Biol. 2001; 79(12):986-92. DOI: 10.1078/0171-9335-00127. View