関: N-glycosidase F、peptide N-glycosidase、peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

WordNet

the 14th letter of the Roman alphabet (同)n

PrepTutorEJDIC

nitrogenの化学記号
neodymiumの化学記号

English Journal

ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase.

Park S1, Jang I, Zuber C, Lee Y, Cho JW, Matsuo I, Ito Y, Roth J.Author information 1WCU Program, Department of Integrated OMICS for Biomedical Science, Yonsei University Graduate School, Seoul, 120-749, Korea.AbstractER degradation-enhancing α-mannosidase-like 1 protein (EDEM1) is involved in the routing of misfolded glycoproteins for degradation in the cytoplasm. Previously, we reported that EDEM1 leaves the endoplasmic reticulum via non-COPII vesicles (Zuber et al. in Proc Natl Acad Sci USA 104:4407-4412, 2007) and becomes degraded by basal autophagy (Le Fourn et al. in Cell Mol Life Sci 66:1434-1445, 2009). However, it is unknown which type of autophagy is involved. Likewise, how EDEM1 is targeted to autophagosomes remains elusive. We now show that EDEM1 is degraded by selective autophagy. It colocalizes with the selective autophagy cargo receptors p62/SQSTM1, neighbor of BRCA1 gene 1 (NBR1) and autophagy-linked FYVE (Alfy) protein, and becomes engulfed by autophagic isolation membranes. The interaction with p62/SQSTM1 and NBR1 is required for routing of EDEM1 to autophagosomes since it can be blocked by short inhibitory RNA knockdown of the cargo receptors. Furthermore, p62/SQSTM1 interacts only with deglycosylated EDEM1 that is also ubiquitinated. The deglycosylation of EDEM1 occurs by the cytosolic peptide N-glycanase and is a prerequisite for interaction and aggregate formation with p62/SQSTM1 as demonstrated by the effect of peptide N-glycanase inhibitors on the formation of protein aggregates. Conversely, aggregation of p62/SQSTM1 and EDEM1 occurs independent of cytoplasmic histone deacetylase. These data provide novel insight into the mechanism of autophagic degradation of the ER-associated protein degradation (ERAD) component EDEM1 and disclose hitherto unknown parallels with the clearance of cytoplasmic aggregates of misfolded proteins by selective autophagy.
Histochemistry and cell biology.Histochem Cell Biol.2014 Mar 25. [Epub ahead of print]
ER degradation-enhancing α-mannosidase-like 1 protein (EDEM1) is involved in the routing of misfolded glycoproteins for degradation in the cytoplasm. Previously, we reported that EDEM1 leaves the endoplasmic reticulum via non-COPII vesicles (Zuber et al. in Proc Natl Acad Sci USA 104:4407-4412, 200
PMID 24664425

Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathway.

Enns GM1, Shashi V2, Bainbridge M3, Gambello MJ4, Zahir FR5, Bast T6, Crimian R2, Schoch K2, Platt J1, Cox R1, Bernstein JA1, Scavina M7, Walter RS8, Bibb A4, Jones M4, Hegde M4, Graham BH3, Need AC9, Oviedo A10, Schaaf CP11, Boyle S12, Butte AJ12, Chen R12, Clark MJ12, Haraksingh R12, Cowan TM13, He P14, Langlois S5, Zoghbi HY15, Snyder M12, Gibbs RA16, Freeze HH14, Goldstein DB17.Author information 1Department of Pediatrics, Division of Medical Genetics, Lucile Packard Children's Hospital, Stanford University, Stanford, California, USA.2Department of Pediatrics, Division of Medical Genetics, Duke University, Durham, North Carolina, USA.3Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, USA.4Department of Human Genetics, Division of Medical Genetics, Emory University School of Medicine, Atlanta, Georgia, USA.5Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada.6Epilepsy Centre Kork, Kehl, Germany.7Division of Pediatric Neurology, Department of Pediatrics, Nemours/Alfred I. duPont Hospital for Children, Wilmington, Delaware, USA.8Division of Developmental Medicine, Department of Pediatrics, Nemours/Alfred I. duPont Hospital for Children, Wilmington, Delaware, USA.9Department of Medicine, Imperial College, London, UK.10Department of Pathology and Laboratory Medicine, Dalhousie University, Halifax, Nova Scotia, Canada.111] Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, USA [2] Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, Texas, USA.12Department of Genetics, Stanford University, Stanford, California, USA.13Department of Pathology, Stanford University, Stanford, California, USA.14Sanford-Burnham Medical Research Institute, La Jolla, California, USA.151] Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, USA [2] Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, Texas, USA [3] Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas, USA.161] Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, USA [2] Human Genome Sequencing Center, Baylor College of Medicine, Houston, Texas, USA.171] Center for Human Genome Variation and Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA [2] Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, North Carolina, USA.AbstractPurpose:The endoplasmic reticulum-associated degradation pathway is responsible for the translocation of misfolded proteins across the endoplasmic reticulum membrane into the cytosol for subsequent degradation by the proteasome. To define the phenotype associated with a novel inherited disorder of cytosolic endoplasmic reticulum-associated degradation pathway dysfunction, we studied a series of eight patients with deficiency of N-glycanase 1.Methods:Whole-genome, whole-exome, or standard Sanger sequencing techniques were employed. Retrospective chart reviews were performed in order to obtain clinical data.Results:All patients had global developmental delay, a movement disorder, and hypotonia. Other common findings included hypolacrima or alacrima (7/8), elevated liver transaminases (6/7), microcephaly (6/8), diminished reflexes (6/8), hepatocyte cytoplasmic storage material or vacuolization (5/6), and seizures (4/8). The nonsense mutation c.1201A>T (p.R401X) was the most common deleterious allele.Conclusion:NGLY1 deficiency is a novel autosomal recessive disorder of the endoplasmic reticulum-associated degradation pathway associated with neurological dysfunction, abnormal tear production, and liver disease. The majority of patients detected to date carry a specific nonsense mutation that appears to be associated with severe disease. The phenotypic spectrum is likely to enlarge as cases with a broader range of mutations are detected.Genet Med advance online publication 20 March 2014Genetics in Medicine (2014); doi:10.1038/gim.2014.22.
Genetics in medicine : official journal of the American College of Medical Genetics.Genet Med.2014 Mar 20. doi: 10.1038/gim.2014.22. [Epub ahead of print]
Purpose:The endoplasmic reticulum-associated degradation pathway is responsible for the translocation of misfolded proteins across the endoplasmic reticulum membrane into the cytosol for subsequent degradation by the proteasome. To define the phenotype associated with a novel inherited disorder of c
PMID 24651605

N-Terminal signal sequence is required for cellular trafficking and hyaluronan-depolymerization of KIAA1199.

Yoshida H1, Nagaoka A2, Nakamura S2, Tobiishi M2, Sugiyama Y2, Inoue S2.Author information 1Innovative Beauty Science Laboratory, Kanebo Cosmetics Inc., 3-28, 5-chome, Kotobuki-cho, Odawara-shi, Kanagawa 250-0002, Japan. Electronic address: yoshida.hiroyuki@kanebocos.co.jp.2Innovative Beauty Science Laboratory, Kanebo Cosmetics Inc., 3-28, 5-chome, Kotobuki-cho, Odawara-shi, Kanagawa 250-0002, Japan.AbstractRecently, we disclosed that KIAA1199-mediated hyaluronan (HA) depolymerization requires an acidic cellular microenvironment (e.g. clathrin-coated vesicles or early endosomes), but no information about the structural basis underlying the cellular targeting and functional modification of KIAA1199 was available. Here, we show that the cleavage of N-terminal 30 amino acids occurs in functionally matured KIAA1199, and the deletion of the N-terminal portion results in altered intracellular trafficking of the molecule and loss of cellular HA depolymerization. These results suggest that the N-terminal portion of KIAA1199 functions as a cleavable signal sequence required for proper KIAA1199 translocation and KIAA1199-mediated HA depolymerization.
FEBS letters.FEBS Lett.2014 Jan 3;588(1):111-6. doi: 10.1016/j.febslet.2013.11.017. Epub 2013 Nov 20.
Recently, we disclosed that KIAA1199-mediated hyaluronan (HA) depolymerization requires an acidic cellular microenvironment (e.g. clathrin-coated vesicles or early endosomes), but no information about the structural basis underlying the cellular targeting and functional modification of KIAA1199 was
PMID 24269685

Japanese Journal

Double-Knockout of Putative Endo-β-N-acetylglucosaminidase (ENGase) Genes in Arabidopsis thaliana : Loss of ENGase Activity Induced Accumulation of High-Mannose Type Free N-Glycans Bearing N,N'-Acetylchitobiosyl Unit

KIMURA Yoshinobu,TAKEOKA Yuki,INOUE Masami,MAEDA Megumi,FUJIYAMA Kazuhito
Bioscience, biotechnology, and biochemistry 75(5), 1019-1021, 2011-05-23
… Endo-β-N-acetylglucosaminidase (ENGase) is involved in the production of high-mannose type free N-glycans during plant development and fruit maturation. … The mutant showed no ENGase activity, but produced high-mannose type free N-glycans carrying the N,N′-acetylchitobiosyl unit that is produced by peptide:N-glycanase, indicating that both these genes encode Arabidopsis ENGase. …
NAID 10028273128

担子菌の産生するアスパラギン結合型糖鎖遊離酵素系

濱口祐,井上裕香子,伊藤司 [他]
応用糖質科学 1(2), 159-167, 2011
NAID 40018823736

Related Pictures

role for N ‐glycanase in the cytosolic of PNGaseF on some N -linked glycoproteins glycosylation catalyzed by N-glycanase グリカン調製 Reaction mechanisms of N -glycanase Pedigrees of N - glycanase 1 (NGLY1

★リンクテーブル★

リンク元	「N-グリカナーゼ」「peptide N-glycosidase」「N-glycosidase F」「peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase」
関連記事	「n」「N」「Nd」