Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/38643
Title: ELUCIDATING THE FUNCTION OF GOLPH3 IN MAMMALIAN GLYCOSYLATION
Authors: NATASHA ANN PEREIRA
Keywords: GOLPH3, GOLPH3L, glycosylation, POMGnT1, dystroglycan, Muscle-Eye Brain disease,
Issue Date: 4-Dec-2012
Source: NATASHA ANN PEREIRA (2012-12-04). ELUCIDATING THE FUNCTION OF GOLPH3 IN MAMMALIAN GLYCOSYLATION. ScholarBank@NUS Repository.
Abstract: We screened for novel interacting partners of GOLPH3 and its isoform GOLPH3L through the utilization of a T7 phage display system. Both proteins were found to bind the stem region of human protein O-linked mannose beta-1, 2-N-actetlyglucosaminyltransferase 1 (POMGnT1). These interactions were verified in vitro and in addition, the GOLPH3 proteins and POMGnT1 were shown to co-localize at the Golgi. Importantly we show that loss of this interaction correlated with the inability of POMGnT1 to localize to the Golgi. We demonstrated that the RNAi-mediated knockdown of GOLPH3 and GOLPH3L reduced the functional glycosylation of a-dystroglycan, a glycoprotein which constitutes the dystrophin glycoprotein complex present in the sarcolemma of muscle fibres. Previous studies showed that mutations in POMGnT1 lead to muscle-eye-brain disease (MEB). We discovered that three single missense mutations in the stem domain of POMGnT1 previously described in MEB patients exhibited reduced binding to GOLPH3 and failed to display Golgi localization.
URI: http://scholarbank.nus.edu.sg/handle/10635/38643
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