Moving the O-glycoproteome from form to function

Baenziger, Jacques U.

doi:10.1073/pnas.1206735109

Cited by 6 publications

(3 citation statements)

References 10 publications

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“…In addition to glycosylation, apoC-III can also be C-terminal truncated (des-Ala and des-Ala-Ala), which further increases the number of isoforms (Bondarenko et al 1999;Jin and Manabe 2005;Nicolardi et al 2013a). Interestingly, novel results strongly suggest that glycosylation of apoC-III is an important event in the regulation of lipid metabolism (Holleboom et al 2011;Baenziger 2012). Thus, apoC-III is exclusively glycosylated by GalNAc transferase 2 (GALNT2) (Holleboom et al 2011;Schjoldager et al 2012), and heterozygotes with a loss-of-function mutation in GALNT2 present with an altered apoC-III isoform pattern with more of the non-sialylated variant and less of the monosialylated variant, while the total apoC-III plasma concentration was about the same as compared to wild-type controls (Holleboom et al 2011).…”

Section: Protein Isoforms Translational and Posttranslationalmentioning

confidence: 99%

Structure of HDL: Particle Subclasses and Molecular Components

Kontush

Lindahl

Lhomme

et al. 2014

Handbook of Experimental Pharmacology

227

226

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Section: Protein Isoforms Translational and Posttranslationalmentioning

confidence: 99%

Structure of HDL: Particle Subclasses and Molecular Components

Kontush

Lindahl

Lhomme

et al. 2014

Handbook of Experimental Pharmacology

227

226

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“…However, the functional roles of GALNTs identified to date in cancer are mostly limited to their involvement in cancer cell motility or growth151718192021. Furthermore, the potential function of GALNTs on cancer progression, especially in site-specific metastasis, is poorly understood.…”

mentioning

confidence: 99%

GALNT14 promotes lung-specific breast cancer metastasis by modulating self-renewal and interaction with the lung microenvironment

et al. 2016

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Some polypeptide N-acetyl-galactosaminyltransferases (GALNTs) are associated with cancer, but their function in organ-specific metastasis remains unclear. Here, we report that GALNT14 promotes breast cancer metastasis to the lung by enhancing the initiation of metastatic colonies as well as their subsequent growth into overt metastases. Our results suggest that GALNT14 augments the self-renewal properties of breast cancer cells (BCCs). Furthermore, GALNT14 overcomes the inhibitory effect of lung-derived bone morphogenetic proteins (BMPs) on self-renewal and therefore facilitates metastasis initiation within the lung microenvironment. In addition, GALNT14 supports continuous growth of BCCs in the lung by not only inducing macrophage infiltration but also exploiting macrophage-derived fibroblast growth factors (FGFs). Finally, we identify KRAS-PI3K-c-JUN signalling as an upstream pathway that accounts for the elevated expression of GALNT14 in lung-metastatic BCCs. Collectively, our findings uncover an unprecedented role for GALNT14 in the pulmonary metastasis of breast cancer and elucidate the underlying molecular mechanisms.

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“…Another mutation S371A/V reflects a selective sweep in Netrin-G2 protein from primates to hominins within a similar to T346A functional context when a hydrophobic alanine (in chimpanzee, A)/valine (in marmoset, V) is replaced by a polar serine (S) and a strong positive predictions for glycosylation but not phosphorylation (see SM). This poses a question about whether these two human-specific protein substitutions are associated with advanced cognitive traits as they may represent a hidden layer of poorly studied so far protein glycosylationassociated regulatomes known to affect the brain function and diseases [61,62]. In addition, T346 is nested on exon 5, just 20 nucleotides away from the rs2274855 mutation allele, affecting WM scores [1], and, together with S371A/V, they are both located within the lowest percent identity area (exons (5-7)) of Netrin-Gs (Figure 3C) and are proposed to contribute to NTNG duplicates SF.…”

Section: Evolution Of the Protein Paralogs Encoded By The Ntngsmentioning

confidence: 99%

Cognitive domains function complementation by NTNG gene paralogs

Prosselkov¹,

Polygalov²,

Zhang³

et al. 2016

Biomed Genet Genomics

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A pair of gene paralogs, NTNG1 and NTNG2, sharing identical gene and protein structures and encoding similar proteins, forms a functional complement subfunctionalising (SF) within cognitive domains and forming cognitive endophenotypes, as detected by Intellectual Quotient tests [1]. Both NTNG paralogs are associated with autism spectrum disorder, bipolar disorder and schizophrenia, with unique non-overlapping segregation among the other cognitive disorders, emphasizing an evolutionary gain-dependent link between advanced cognitive functions and concomitant neurocognitive pathologies. We revealed complementary expression and transcriptome composition of the paralogs within the human brain explaining the observed phenomena of NTNG1 and NTNG2 functional complementarity. The gene paralogs expression levels undergo age-dependent and brain area-specific modalities over the almost entire human lifespan. It has also been reported that NTNG1 contains anthropoid-specific constrained regions, and both genes contain non-coding conserved sequences that underwent accelerated evolution in human. NTNG paralogs SF perturbates "structure drives function" concept at protein and gene levels. We suggest that the paralogs function diversification forms a so-called "Cognitive Complement", as an end product of gene duplication and subsequent cognitive subfunction bifurcation among the NTNG gene duplicates.

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Moving the O-glycoproteome from form to function

Cited by 6 publications

References 10 publications

Structure of HDL: Particle Subclasses and Molecular Components

Structure of HDL: Particle Subclasses and Molecular Components

GALNT14 promotes lung-specific breast cancer metastasis by modulating self-renewal and interaction with the lung microenvironment

Cognitive domains function complementation by NTNG gene paralogs

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