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Dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit

DPM1, MPDS, dolichol phosphate mannose synthase, Dpm1p
Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, CD45, Cho, HAD
Papers on DPM1
Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis.
Mancia et al., New York City, United States. In Nat Commun, Dec 2015
The enzymes that perform these reactions, polyisoprenyl-glycosyltransferases (PI-GTs) include dolichol phosphate mannose synthase (DPMS), which generates the mannose donor for glycosylation in the endoplasmic reticulum.
Dolichol phosphate mannose synthase from the pathogenic yeast Candida albicans is a multimeric enzyme.
Palamarczyk et al., Warsaw, Poland. In Biochim Biophys Acta, Nov 2015
BACKGROUND: Dolichol phosphate mannose synthase (DPMS) is a key enzyme in N- and O-linked glycosylations and glycosylphosphatidylinositol (GPI)-anchor synthesis.
Toward the development of transcriptional biodosimetry for the identification of irradiated individuals and assessment of absorbed radiation dose.
Kruszewski et al., Warsaw, Poland. In Radiat Environ Biophys, Aug 2015
The mRNA level of 16 genes (ATF3, BAX, BBC3, BCL2, CDKN1A, DDB2, FDXR, GADD45A, GDF15, MDM2, PLK3, SERPINE1, SESN2, TNFRSF10B, TNFSF4, and VWCE) was assessed by reverse transcription quantitative PCR 6, 12, 24, and 48 h after exposure with ITFG1 and DPM1 used as a reference genes.
Predictability of the Call Triage Protocol to Detect if Dispatchers Should Activate Community First Responders.
Iijima et al., Tokyo, Japan. In Prehosp Disaster Med, 2014
CONCLUSION: Two call triage protocols have almost the same predictability as the Medical Priority Dispatch System (MPDS).
Congenital disorders of glycosylation with emphasis on cerebellar involvement.
Jaeken et al., Catania, Italy. In Semin Neurol, 2014
It has also been reported in some patients with ALG1-CDG, ALG3-CDG, ALG9-CDG, ALG6-CDG, ALG8-CDG, PIGA-CDG, DPM1-CDG, DPM2-CDG, B4GALT1-CDG, SLC35A2-CDG, COG1-CDG, COG5-CDG, COG7-CDG, and COG8-CDG.
Prognostic relevance of glycosylation-associated genes in breast cancer.
Müller et al., Hamburg, Germany. In Breast Cancer Res Treat, 2014
In the second cohort, six of the 24 relevant genes were of prognostic significance (FUT1, FUCA1, POFUT1, MAN1A1, RPN1 and DPM1), whereas a trend was observed for three additional probesets (GCNT4, ST3GAL6 and UGCG).
Comparison of Medical Priority Dispatch (MPD) and Criteria Based Dispatch (CBD) relating to cardiac arrest calls.
Wik et al., Oslo, Norway. In Resuscitation, 2014
RESULTS: The MPDS-site processed 182 cardiac arrest calls and the CBD-site 232, of which 100 and 140 calls met the inclusion criteria, respectively.
Ethanol-induced impairment in the biosynthesis of N-linked glycosylation.
Hülsmeier et al., Zürich, Switzerland. In J Cell Biochem, 2014
Transcript analysis of genes involved in N-glycosylation showed a 17% decrease in expression levels of DPM1, a subunit of the dolichol-phosphate-mannose synthase, and an 8% increase in RPN2, a subunit of the oligosaccharyl transferase.
[cAMP cascade in regulation of protein glycosylation].
Janik et al., In Postepy Biochem, 2013
N-glycosylation starts with the formation of lipid-linked oligosaccharides and this process is catalysed by crucial glycosyltransferase - dolichol phosphate mannose synthase.
Disrupting KATP channels diminishes the estrogen-mediated protection in female mutant mice during ischemia-reperfusion.
Shi et al., New York City, United States. In Clin Proteomics, 2013
Additional time-point experiments revealed that I-R hearts had increased levels of N-glycosylated SUR2; and DPM1, the first committed step enzyme in the N-glycosylation pathway.
Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy.
Mehta et al., New York City, United States. In Mol Genet Metab, 2013
Carbohydrate deficient transferrin testing showed a pattern pointing to a CDG type I. Sanger sequencing of DPM1 (dolichol-P-mannose synthase subunit 1) revealed a novel Gly > Val change c.455G > T missense mutation resulting in p.Gly152Val) of unknown pathogenicity and deletion/duplication analysis revealed an intragenic deletion from exons 3 to 7 on the other allele.
Quantification of individual proteins in silicone hydrogel contact lens deposits.
Willcox et al., Sydney, Australia. In Mol Vis, 2012
Higher amounts of proteins were extracted from lenses after wear when they were used with an MPDS containing polyhexamethylene biguanide (PHMB) and poloxamer 407 compared with MPDSs containing polyquaternium-1 (PQ-1)/alexidine dihydrochloride with Tetronic 904 or PQ-1/ PHMB with poloxamine and sulfobetaine (p < 0.05).
Defect in dolichol-dependent glycosylation increases sensitivity of Saccharomyces cerevisiae towards anti-fungal drugs.
Palamarczyk et al., Warsaw, Poland. In Yeast, 2010
Two temperature-sensitive Saccharomyces cerevisiae mutants, sec59-1 and dpm1-6, impaired, respectively, in dolichol kinase (Sec59p) and dolichyl phosphate mannose (DolPMan) synthase (Dpm1p), have an aberrant cell wall structure and composition.
Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides.
Hennet et al., Zürich, Switzerland. In Hum Mutat, 2009
This review sets the state of the art by listing all mutations identified in the 15 genes (PMM2, MPI, DPAGT1, ALG1, ALG2, ALG3, ALG9, ALG12, ALG6, ALG8, DOLK, DPM1, DPM3, MPDU1, and RFT1) that yield a deficiency of dolichol-linked oligosaccharide biosynthesis.
Protein glycosylation in Candida.
López-Romero et al., Aberdeen, United Kingdom. In Future Microbiol, 2009
Here, we refer to studies dealing with the identification and characterization of enzymes such as dolichol phosphate mannose synthase, dolichol phosphate glucose synthase and processing glycosidases and synthesis, structure and recognition of mannans and discuss recent findings in the context of Candida albicans pathogenesis.
Inhibition of glycosyltransferase activities as the basis for drug development.
Brockhausen et al., Kingston, Canada. In Methods Mol Biol, 2008
Another example is the use of a class of amino acid specific reagents as inhibitors that help to obtain information about amino acid residues at or near the active site of dolichol-phosphate-mannose synthase or those involved in the enzyme mechanism.
Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions.
Palamarczyk et al., Warsaw, Poland. In Yeast, 2007
Evidence is presented that temperature-sensitive Saccharomyces cerevisiae mutants, impaired in dolichol kinase (Sec59p) or dolichyl phosphate mannose synthase (Dpm1p) activity have an aberrant cell wall composition and ultrastructure.
Structural studies and mechanism of Saccharomyces cerevisiae dolichyl-phosphate-mannose synthase: insights into the initial step of synthesis of dolichyl-phosphate-linked oligosaccharide chains in membranes of endoplasmic reticulum.
Jedrzejas et al., Oakland, United States. In Glycobiology, 2006
A three-dimensional (3D) model of the enzyme was produced with bound substrates, Dol-P, GDP-Man, and divalent cations to delineate the binding sites for these substrates as well as the catalytic site.
In vitro phosphorylation by cAMP-dependent protein kinase up-regulates recombinant Saccharomyces cerevisiae mannosylphosphodolichol synthase.
Baksi et al., San Juan, Puerto Rico. In J Biol Chem, 2005
S. cerevisiae DPMS activity is regulated by the cAMP-dependent protein phosphorylation signal, and the phosphorylation target is serine 141
Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p.
Mayinger et al., Portland, United States. In J Cell Biol, 2005
Interaction of Dpm1p with Sac1p persists during exponential cell division but is rapidly abolished when cell growth slows.
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