Dataset Information

CHO O-Mannosylation independent of POMT1/2

ABSTRACT: Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserved O-Man glycans in specific EC domains, and it was suggested that the function of E-Cadherin was dependent on the O-Man glycans. Deficiencies in the two human polypeptide O-mannosyltransferases, POMT1 and T2, underlie a subgroup of congenital muscular dystrophies (CMD) designated α-dystroglycanopathies, because deficient O-Man glycans on -dystroglycan impair laminin interaction with -dystroglycan and the dystrophin complex. In order to explore the functions of O-Man glycans on cadherins and protocadherins we used a combinatorial gene editing strategy in multiple cell lines to evaluate to the role of the two POMTs initiation O-Man glycosylation and the major enzyme elongating O-Man glycans, the POMGNT1 2GlcNAc-transferase. Surprisingly, we discovered that O-Man glycans on cadherins and protocadherins do not appear to require POMT1 and T2 and moreover that the O-Man glycans on these proteins are not elongated in contrast to those on dystroglycan.

INSTRUMENT(S): Orbitrap Fusion ETD, LTQ Orbitrap Velos

ORGANISM(S): Cricetulus Griseus (chinese Hamster) (cricetulus Barabensis Griseus)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Adnan Halim

LAB HEAD: Henrik Clausen

PROVIDER: PXD004341 | Pride | 2017-05-18

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	130828_Ida_CHO_wt_ETD_SUB_4xHex.msf	Msf
	130828_Ida_CHO_wt_F17_3HCD_ETD.raw	Raw
	130828_Ida_CHO_wt_F18_3HCD_ETD.raw	Raw
	130828_Ida_CHO_wt_F19_3HCD_ETD.raw	Raw
	130828_Ida_CHO_wt_F20_3HCD_ETD.raw	Raw

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Publications

Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.

Larsen Ida Signe Bohse ISB Narimatsu Yoshiki Y Joshi Hiren Jitendra HJ Yang Zhang Z Harrison Oliver J OJ Brasch Julia J Shapiro Lawrence L Honig Barry B Vakhrushev Sergey Y SY Clausen Henrik H Halim Adnan A

The Journal of biological chemistry 20170516 27

Protein O-mannosylation is found in yeast and metazoans, and a family of conserved orthologous protein O-mannosyltransferases is believed to initiate this important post-translational modification. We recently discovered that the cadherin superfamily carries O-linked mannose (O-Man) glycans at highly conserved residues in specific extracellular cadherin domains, and it was suggested that the function of E-cadherin was dependent on the O-Man glycans. Deficiencie ...[more]

PMID: 28512129

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Project description:Streptococcus pneumoniae is a strictly fermentative human pathogen that relies on carbohydrate metabolism to generate energy for growth. The nasopharynx colonised by the bacterium is poor in free sugars, but mucosa lining glycans can provide a source of sugar. In blood and inflamed tissues glucose is the prevailing sugar. As a result during progression from colonisation to disease S. pneumoniae has to cope with a pronounced shift in carbohydrate nature and availability. Thus, we set out to assess the pneumococcal response to sugars found in glycans and the influence of glucose (Glc) on this response at the transcriptional, physiological and metabolic levels. Galactose (Gal), N-acetylglucosamine (GlcNAc) and mannose (Man) affected the expression of 8 to 14% of the genes covering cellular functions including central carbon metabolism and virulence. The pattern of end-products as monitored by in vivo 13C-NMR is in good agreement with the fermentation profiles during growth, while the pools of phosphorylated metabolites are consistent with the type of fermentation observed (homolactic vs. mixed) and regulation at the metabolic level. Furthermore, the accumulation of -Gal6P and Man6P indicate metabolic bottlenecks in the metabolism of Gal and Man, respectively. Glc added to cells actively metabolizing other sugar(s)was readily consumed and elicited a metabolic shift towards a homolactic profile. The transcriptional response to Glc was large (over 5% of the genome). In central carbon metabolism (most represented category), Glc exerted mostly negative regulation. The smallest response was observed on a sugar mix, suggesting that exposure to varied sugars improves the fitness of S. pneumoniae. The expression of classical virulence factors was negatively controlled by Glc in a sugar-dependent manner. Overall, our results shed new light on the link between carbohydrate metabolism, adaptation to host niches and virulence. Two conditions with the same strain (D39), including a dye swap

Dataset Information

CHO O-Mannosylation independent of POMT1/2

Dataset's files

Publications

Mammalian <i>O</i>-mannosylation of cadherins and plexins is independent of protein <i>O</i>-mannosyltransferases 1 and 2.

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