| Autor: |
Willett RA; Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR, USA., Pokrovskaya ID, Lupashin VV |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2013; Vol. 1022, pp. 61-72. |
| DOI: |
10.1007/978-1-62703-465-4_6 |
| Abstrakt: |
Staining of molecules such as proteins and glycoconjugates allows for an analysis of their localization within the cell and provides insight into their functional status. Glycosyltransferases, a class of enzymes which are responsible for glycosylating host proteins, are mostly localized to the Golgi apparatus, and their localization is maintained in part by a protein vesicular tethering complex, the conserved oligomeric Golgi (COG) complex. Here we detail a combination of fluorescent lectin and immuno-staining in cells depleted of COG complex subunits to examine the status of Golgi glycosyltransferases. The combination of these techniques allows for a detailed characterization of the changes in function and localization of Golgi glycosyltransferases with respect to transient COG subunit depletion. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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