Golgi Phosphoprotein 3 Regulates the Physical Association of Glycolipid Glycosyltransferases †

RUGGIERO, FERNANDO M.; MARTÍNEZ-KOTESKI, NATALIA; FIDELIO, GERARDO D.; VILCAES, ALDO A.; DANIOTTI, JOSE L.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

MDPI

Año: 2022 vol. 23

1661-6596

lycolipid glycosylation is an intricate process that mainly takes place in the Golgi by the complex interplay between glycosyltransferases. Several features such as the organization, stoichiometry and composition of these complexes may modify their sorting properties, sub-Golgi localization, enzymatic activity and in consequence, the pattern of glycosylation at the plasma membrane. In spite of the advance in our comprehension about physiological and pathological cellular states of glycosylation, the molecular basis underlying the metabolism of glycolipids and the players involved in this process remain not fully understood. In the present work, using biochemical and fluorescence microscopy approaches, we demonstrate the existence of a physical association between two ganglioside glycosyltransferases, namely, ST3Gal-II (GD1a synthase) and β3GalT-IV (GM1 synthase) with Golgi phosphoprotein 3 (GOLPH3) in mammalian cultured cells. After GOLPH3 knockdown, the localization of both enzy