Murine UDP-GlcNAc:Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase lacking the γ-subunit retains substantial activity toward acid hydrolases

Wang Sik Lee, Bobby Joe Payne, Claire M. Gelfman, Peter Vogel, Stuart Kornfeld

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phosphotransferase) mediates the first step in the synthesis of the mannose 6-phosphate recognition markeronacidhydrolases.Thetransferaseexistsasan α2β2γ2 hexameric complex with the α- and β-subunits derived from a single precursor molecule. The catalytic function of the transferase is attributed to the α- and β-subunits, whereas the γ-subunit is believed to be involved in the recognition of a conformation-dependent protein determinant common to acid hydrolases. Using knock-out mice with mutations in either the α/β gene or the γ gene, we show that disruption of the α/β gene completely abolishes phosphorylation of high mannose oligosaccharides on acid hydrolases whereas knock-out of the γ gene results in only a partial loss of phosphorylation. These findings demonstrate that the α/β-subunits, in addition to their catalytic function, have some ability to recognize acid hydrolases as specific substrates. This process is enhanced by the γ-subunit.

Original languageEnglish
Pages (from-to)27198-27203
Number of pages6
JournalJournal of Biological Chemistry
Volume282
Issue number37
DOIs
StatePublished - Sep 14 2007

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