Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p family of  -1,3-mannosyltransferases responsible for adding the terminal mannose residues of O-linked oligosaccharides

Romero, Pedro; Lussier, Marc; Véronneau, Steeve; Sdicu, Anne‐Marie; Herscovics, Annetté; Bussey, Howard

doi:10.1093/glycob/9.10.1045

Cited by 57 publications

(42 citation statements)

References 32 publications

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“…Transfer of the first two a1,2-Man is carried out by the Ktr1 subfamily members Ktr1, Ktr3, and Kre2 and extension of the trisaccharide chain with one or two a1,3-linked Man by Mnn1 family members Mnn1, Mnt2, and Mnt3 (Lussier et al 1997a;Romero et al 1999). The second a1,2-Man of an O-linked glycan can be modified with Man-1-P by Mnn6 with the involvement of the regulator Mnn4 (Nakayama et al 1998).…”

Section: O-mannosylationmentioning

confidence: 99%

“…Extension of the trisaccharide chain with one or two α1,3--linked Man is the shared responsibility of Mnn1 family members Mnn1, Mnt2, and Mnt3, with Mnn1 having the major role in adding the fourth Man but Mnt2 and Mnt3 dominating when the fifth is added (Romero et al 1999). Mnn1 also transfers Man to N--linked outer chains.…”

Section: Mannan Elaboration In the Golgi)mentioning

confidence: 99%

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Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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The wall gives a Saccharomyces cerevisiae cell its osmotic integrity; defines cell shape during budding growth, mating, sporulation, and pseudohypha formation; and presents adhesive glycoproteins to other yeast cells. The wall consists of b1,3-and b1,6-glucans, a small amount of chitin, and many different proteins that may bear N-and O-linked glycans and a glycolipid anchor. These components become cross-linked in various ways to form higher-order complexes. Wall composition and degree of cross-linking vary during growth and development and change in response to cell wall stress. This article reviews wall biogenesis in vegetative cells, covering the structure of wall components and how they are cross-linked; the biosynthesis of N-and O-linked glycans, glycosylphosphatidylinositol membrane anchors, b1,3-and b1,6-linked glucans, and chitin; the reactions that cross-link wall components; and the possible functions of enzymatic and nonenzymatic cell wall proteins. TABLE OF CONTENTS Abstract 775Introduction 777

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Section: O-mannosylationmentioning

confidence: 99%

Section: Mannan Elaboration In the Golgi)mentioning

confidence: 99%

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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“…The latter stage of O-mannosylation in the Golgi has been poorly characterized in most species except for Saccharomyces cerevisiae. In this yeast, the KRE2/MNT1 protein family is responsible for the addition of the second and third mannose residues (Man 2 -Man 3 ) (Lussier et al, 1997a(Lussier et al, , 1997b, and MNN1 family proteins attach a fourth (Man 4 ) and possibly additional mannose residues (Romero et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

TheO-Mannosyltransferase PMT4 Is Essential for Normal Appressorium Formation and Penetration inUstilago maydis

2009

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In Saccharomyces cerevisiae, the PMT, KRE2/MNT1, and MNN1 mannosyltransferase protein families catalyze the steps of the O-mannosylation pathway, sequentially adding mannoses to target proteins. We have identified members of all three families and analyzed their roles in pathogenesis of the maize smut fungus Ustilago maydis. Furthermore, we have shown that PMT4, one of the three PMT family members in U. maydis, is essential for tumor formation in Zea mays. Significantly, PMT4 seems to be required only for pathogenesis and is dispensable for other aspects of the U. maydis life cycle. We subsequently show that the deletion of pmt4 results in a strong reduction in the frequency of appressorium formation, with the few appressoria that do form lacking the capacity to penetrate the plant cuticle. Our findings suggest that the O-mannosylation pathway plays a key role in the posttranslational modification of proteins involved in the pathogenic development of U. maydis. The fact that PMT homologs are not found in plants may open new avenues for the development of fungal control strategies. Moreover, the discovery of a highly specific requirement for a single O-mannosyltransferase should aid in the identification of the proteins directly involved in fungal plant penetration, thus leading to a better understanding of plant-fungi interactions.

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“…α-1,6-mannose outer chain with α-1,2-mannose branches is terminated by the addition of α-1,3-mannose by α-1,3-mannosyltransferases Mnt2p, Mnt3p, Mnt4p and Mnn1p (Romero et al, 1999;Yip et al, 1994). All these mannosyltransferases are type-II membrane proteins and their catalytic domains localize in the Golgi lumen.…”

mentioning

confidence: 99%

Localization of GDP-mannose transporter in the Golgi requires retrieval to the endoplasmic reticulum depending on its cytoplasmic tail and coatomer

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et al. 2004

Journal of Cell Science

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IntroductionIn the eukaryotic cell, the secretory proteins are transported to the cell surface through the endoplasmic reticulum (ER) and Golgi apparatus. During the transport process, most of the secretory proteins are modified by oligosaccharides. The initial transfer of carbohydrate to the polypeptide from dolichol-sugar intermediates occurs in the ER and further addition and modification of oligosaccharides occurs mainly in the Golgi. The Golgi glycosylation is conducted by a variety of glycosyltransferases and the donor substrate is nucleotidesugar. The nucleotide-sugar is synthesized in the cytoplasm and incorporated in the Golgi lumenal space by a specific nucleotide-sugar transporter (NST).In the Golgi of Saccharomyces cerevisiae, the glycosylation occurs solely by mannose and GDP-mannose is the essential substrate of various mannosyltransferases. Several Golgi mannosyltransferases have been identified. Och1p is the crucial α-1,6-mannosyltransferase, which initiates the elongation of outer mannosyl chain of the N-oligosaccharide core (Nakanishi-Shindo et al., 1993). Two hetero-oligomeric complexes that contain Mnn9p as a common subunit, Mnn9p-Van1p and Mnn9p-Anp1p-Hoc1p-Mnn10p-Mnn11p [named MTase I and II by Jungmann et al. (Jungmann et al., 1999) or the V and A complexes by Kojima et al. (Kojima et al., 1999), respectively], transfer either α-1,6-or α-1,2-mannose to the acceptor N-glycosyl groups (Jungmann and Munro, 1998). The latter complex might also participate in elongation of Omannosyl groups (Kojima et al., 1999). Mnt1p, Mnn2p and Mnn3p function as α-1,2-mannosyltransferase (Hausler and Robbins, 1992; Rayner and Munro, 1998). The elongation of α-1,6-mannose outer chain with α-1,2-mannose branches is terminated by the addition of α-1,3-mannose by α-1,3-mannosyltransferases Mnt2p, Mnt3p, Mnt4p and Mnn1p (Romero et al., 1999;Yip et al., 1994). All these mannosyltransferases are type-II membrane proteins and their catalytic domains localize in the Golgi lumen. The GDPmannose transporter (GMT) moves GDP-mannose into the Golgi lumen from the cytosol and moves GMP out. GMT is a member of the NST family (Berninsone and Hirschberg, 2000), which has similar multiple transmembrane domains (TMD) and functions as an antiporter of nucleotide-diphosphate-sugar and nucleotide-monophosphate in the organelle membrane (Abeijon et al., 1996;Eckhardt et al., 1996;Goto et al., 2001;Ma et al., 1997;Miura et al., 1996;Poster and Dean, 1996;Tabuchi et al., 1997).The mannosyltransferases and GMT localize to the Golgi apparatus for precise glycosylation but the mechanism is still not clear. Two models have been proposed for stable localization of membrane protein -the 'kin recognition' model (Nilsson et al., 1994;Nilsson et al., 1993) and the 'lipid bilayer' model (Bretscher and Munro, 1993;Munro, 1995). The kin recognition model proposes that the resident proteins form a large hetero-oligomer by protein-protein interaction in the organelle membrane and are consequently prevented from entering the budding vesicles destine...

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Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p family of -1,3-mannosyltransferases responsible for adding the terminal mannose residues of O-linked oligosaccharides

Cited by 57 publications

References 32 publications

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

TheO-Mannosyltransferase PMT4 Is Essential for Normal Appressorium Formation and Penetration inUstilago maydis

Localization of GDP-mannose transporter in the Golgi requires retrieval to the endoplasmic reticulum depending on its cytoplasmic tail and coatomer

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