Literature DB >> 11886838

Ectopic localizations of Golgi glycosyltransferases.

Eric G Berger1.   

Abstract

Glycosyltransferases involved in N- and O-glycan chain elongation and termination are localized in the Golgi apparatus. Early evidence in support of this rule was based on fractionation techniques and was corroborated by numerous immunocytochemical studies. Usually these studies were confined to cultured cell lines exhibiting little differentiation features, such as HeLa cells. However, localization studies conducted in primary cell cultures (e.g., human umbilical vein endothelial cells), cells obtained ex vivo (e.g., sperm cells), and tissue sections (e.g., intestinal, renal, or hepatic tissue) often reveal ectopic localizations of glycosyltransferases usually at post-Golgi sites, including the plasma membrane. Hence, extracellular cues resulting from specific adhesion sites may influence post-Golgi trafficking routes, which may be reflected by ectopic localization of Golgi enzymes.

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Year:  2002        PMID: 11886838     DOI: 10.1093/glycob/12.2.29r

Source DB:  PubMed          Journal:  Glycobiology        ISSN: 0959-6658            Impact factor:   4.313


  12 in total

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Review 8.  Heme and FLVCR-related transporter families SLC48 and SLC49.

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10.  The dynamics of engineered resident proteins in the mammalian Golgi complex relies on cisternal maturation.

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