The retention mechanism of cell wall proteins in Saccharomyces cerevisiae. Wall-bound Cwp2p is β-1,6-glucosylated

Vaart, J.M. van der; Schagen, Frank S van; Mooren, A. T. A.; Chapman, John W.; Klis, Frans M.; Verrips, C. Theo

doi:10.1016/s0304-4165(96)00067-0

Cited by 37 publications

(33 citation statements)

References 38 publications

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“…As already discussed above, fungal GPI proteins can have two Wnal destinations, either the plasma membrane or the cell wall. Cell wall attachment in S. cerevisiae has been shown to require the processing of the GPI-anchor resulting in attachment of the Wrst mannose residue of the GPI-glycan core to a 1,6--glucan acceptor molecule Lu et al, 1994;Van der Vaart et al, 1996). The biogenesis of the sexual agglutinin Sag1p of S. cerevisiae has been studied in detail (Lu et al, 1994(Lu et al, , 1995.…”

Section: Posttranslational Modiwcations Of Fungal Glycoproteinsmentioning

confidence: 99%

Features and functions of covalently linked proteins in fungal cell walls

Groot

Ram

Klis

2005

Fungal Genetics and Biology

265

250

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Section: Posttranslational Modiwcations Of Fungal Glycoproteinsmentioning

confidence: 99%

Features and functions of covalently linked proteins in fungal cell walls

Groot

Ram

Klis

2005

Fungal Genetics and Biology

265

250

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“…A dual function has been now established for these proteins: some members of this family (such as Gel1p, Gas1p, Phr1p, and Phr2p) have a 1,3-␤-glucanosyltransferase activity responsible for the modification of the existing polymers of the cell wall, whereas others, such as Krep, are involved in the de novo synthesis of new polymers. Some GPIanchored proteins without known enzymatic function (like Ag␣1, Cwp1p, or Cwp2p) are covalently incorporated to the cell wall after cleavage of the GPI anchor and become part of three-dimensional network composed by cell wall polymers (36,42,43).…”

Section: Isolation and Sequence Analysis Of The Gel1 Gene Encoding Thmentioning

confidence: 99%

Glycosylphosphatidylinositol-anchored Glucanosyltransferases Play an Active Role in the Biosynthesis of the Fungal Cell Wall

Mouyna

Fontaine

Vai

et al. 2000

Journal of Biological Chemistry

325

337

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A novel 1,3-␤-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus was recently characterized. This enzyme splits internally a 1,3-␤-glucan molecule and transfers the newly generated reducing end to the non-reducing end of another 1,3-␤-glucan molecule forming a 1,3-␤ linkage, resulting in the elongation of 1,3-␤-glucan chains. The GEL1 gene encoding this enzyme was cloned and sequenced. The predicted amino acid sequence of Gel1p was homologous to several yeast protein families encoded by GAS of Saccharomyces cerevisiae, PHR of Candida albicans, and EPD of Candida maltosa. Although the expression of these genes is required for correct morphogenesis in yeast, the biochemical function of the encoded proteins was unknown. The biochemical assays performed on purified recombinant Gas1p, Phr1p, and Phr2p showed that these proteins have a 1,3-␤-glucanosyltransferase activity similar to that of Gel1p. Biochemical data and sequence analysis have shown that Gel1p is attached to the membrane through a glycosylphosphatidylinositol in a similar manner as the yeast homologous proteins. The activity has been also detected in membrane preparations, showing that this 1,3-␤-glucanosyltransferase is indeed active in vivo. Our results show that transglycosidases anchored to the plasma membrane via glycosylphosphatidylinositols can play an active role in fungal cell wall synthesis.

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“…These phosphodiester bonds probably originate from the GPI anchor (10). In addition to ␣-agglutinin, other proteins that contain a GPI anchor addition signal are covalently associated with the cell wall (26,38,44,45). However, as mentioned above, not all proteins containing a GPI anchor are destined for the cell wall.…”

mentioning

confidence: 99%

Restrictive glycosylphosphatidylinositol anchor synthesis in cwh6/gpi3 yeast cells causes aberrant biogenesis of cell wall proteins

et al. 1997

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We previously reported that the defects in the Saccharomyces cerevisiae cwh6 Calcofluor white-hypersensitive cell wall mutant are caused by a mutation in SPT14/GPI3, a gene involved in glycosylphosphatidylinositol (GPI) anchor biosynthesis. Here we describe the effect of cwh6/spt14/gpi3 on the biogenesis of cell wall proteins. It was found that the release of precursors of cell wall proteins from the endoplasmic reticulum (ER) was retarded. This was accompanied by proliferation of ER structures. The majority of the cell wall protein precursors that eventually left the ER were not covalently incorporated into the cell wall but were secreted into the growth medium. Despite the inefficient incorporation of cell wall proteins, there was no net effect on the protein level in the cell wall. It is postulated that the availability of GPI-dependent cell wall proteins determines the rate of cell wall construction and limits growth rate.

show abstract

The retention mechanism of cell wall proteins in Saccharomyces cerevisiae. Wall-bound Cwp2p is β-1,6-glucosylated

Cited by 37 publications

References 38 publications

Features and functions of covalently linked proteins in fungal cell walls

Features and functions of covalently linked proteins in fungal cell walls

Glycosylphosphatidylinositol-anchored Glucanosyltransferases Play an Active Role in the Biosynthesis of the Fungal Cell Wall

Restrictive glycosylphosphatidylinositol anchor synthesis in cwh6/gpi3 yeast cells causes aberrant biogenesis of cell wall proteins

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