Identification of a site in Sar1 involved in the interaction with the cytoplasmic tail of glycolipid glycosyltransferases.

The Journal of Biological Chemistry
Cristián A QuinteroHugo J F Maccioni

Abstract

Glycolipid glycosyltransferases (GGT) are transported from the endoplasmic reticulum (ER) to the Golgi, their site of residence, via COPII vesicles. An interaction of a (R/K)X(R/K) motif at their cytoplasmic tail (CT) with Sar1 is critical for the selective concentration in the transport vesicles. In this work using computational docking, we identify three putative binding pockets in Sar1 (sites A, B, and C) involved in the interaction with the (R/K)X(R/K) motif. Sar1 mutants with alanine replacement of amino acids in site A were tested in vitro and in cells. In vitro, mutant versions showed a reduced ability to bind immobilized peptides with the CT sequence of GalT2. In cells, Sar1 mutants (Sar1(D198A)) specifically affect the exiting of GGT from the ER, resulting in an ER/Golgi concentration ratio favoring the ER. Neither the typical Golgi localization of GM130 nor the exiting and transport of the G protein of the vesicular stomatitis virus were affected. The protein kinase inhibitor H89 produced accumulation of Sec23, Sar1, and GalT2 at the ER exit sites; Sar1(D189A) also accumulated at these sites, but in this case GalT2 remained disperse along ER membranes. The results indicate that amino acids in site A of Sar1 are involv...Continue Reading

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Citations

Sep 19, 2012·The Journal of Biological Chemistry·Armen PetrosyanPi-Wan Cheng
Oct 1, 2013·Trends in Cell Biology·Rossella VendittiMaria Antonietta De Matteis
Mar 23, 2011·FEBS Letters·Hugo J F MaccioniWaldo Spessott
Aug 29, 2012·Trends in Plant Science·Ai OikawaHenrik V Scheller
Mar 5, 2011·Journal of Neurochemistry·Hugo J F MaccioniMariana L Ferrari
Mar 5, 2016·World Journal of Gastroenterology : WJG·Yu-Tao ZhanWei An
Feb 22, 2021·Current Opinion in Cell Biology·Sha SunJunjie Hu

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