Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins

Меркулова, Т. И.; Lucas, Marguerite; Jabet, Carole; Lamandé, Noël; Rouzeau, Jean-Denis; Gros, François; Lazar, Monique; Keller, Andreas

doi:10.1042/bj3230791

Cited by 72 publications

(94 citation statements)

References 47 publications

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“…In the same way, the observed association of PGM with cytoskeleton in neutrophils may have been due to hereby employed experimental design which involved a phagocytic stimulus. Our result is consistent with the previous report indicating that glycolytic enzymes enolase, aldolase, creatine kinase, pyruvate kinase, and PGM form a complex in rabbit muscle [37]. Thereby, association of PGM with the cytoskeleton may be mediated through other members of this enzyme multiprotein complex such as pyruvate kinase and enolase, whose ability to associate with cytoskeleton is well known [35,36].…”

Section: Cytosolic Skeleton Fractionsupporting

confidence: 93%

Subproteome analysis of the neutrophil cytoskeleton

Crawford

Way

et al. 2009

Proteomics

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Neutrophils play a key role in the early host-defense mechanisms due to their capacity to migrate into inflamed tissues and phagocytose microorganisms. The cytoskeleton has an essential role in these neutrophil functions, however, its composition is still poorly understood. We separately analyzed different cytoskeletal compartments: cytosolic skeleton, phagosome membrane skeleton, and plasma membrane skeleton. Using a proteomic approach, 138 nonredundant proteins were identified. Proteins not previously known to associate with the skeleton were: n-acetylglucosamine kinase, phosphoglycerate mutase 1, prohibitin, ficolin-1, phosphogluconate dehydrogenase, glucosidase, transketolase, major vault protein, valosin-containing protein, aldehyde dehydrogenase, and lung cancer-related protein-8 (LCRP8). The majority of these proteins can be classified as energy metabolism enzymes. Such a finding was interesting because neutrophil energy metabolism is unusual, mainly relying on glycolysis. The enrichment of phosphoglycerate mutase in cytosolic skeleton was additionally indicated by the use of Western blotting. This is the broadest subcellular investigation to date of the neutrophil cytoskeletal proteome and the first proteomic analysis in any cell type of the phagosome skeleton. The association of metabolic enzymes with cytoskeleton is suggestive of the importance of their localized enrichment and macromolecular organization in neutrophils.

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Section: Cytosolic Skeleton Fractionsupporting

confidence: 93%

Subproteome analysis of the neutrophil cytoskeleton

Crawford

Way

et al. 2009

Proteomics

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“…For the ␤-enolase, two different isoforms have been identified on 2D gels. These two isoforms do not correspond to different phosphorylated forms, but are due to the presence or the absence of a C-terminal lysine (40); nevertheless, these two isoforms are both O-linked N-acetylglucosaminylated.…”

Section: Discussionmentioning

confidence: 91%

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

Cieniewski-Bernard

Bastide²,

Lefebvre

et al. 2004

Molecular & Cellular Proteomics

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O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation. O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide ␤-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose. Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach. Fourteen proteins were identified as being O-GlcNAc modified. These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain). A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction. These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.

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“…Most glycolytic enzymes, including PGAM, exist in complexes bound to the microtubule network (26,27). The GTPases Rac and Cdc42 regulate not only F-actin reorganization but also microtubule dynamics through Pak, which phosphorylates and thereby inhibits the microtubule-destabilizing protein stathmin, leading to microtubule stabilization (28).…”

Section: Discussionmentioning

confidence: 99%

A p21-Activated Kinase-controlled Metabolic Switch Up-regulates Phagocyte NADPH Oxidase

Shalom‐Barak

Knaus

2002

Journal of Biological Chemistry

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Chemoattractant-stimulated phagocytes increase their glucose uptake and divert energy production from glycolysis to the pentose phosphate pathway to generate NADPH. NADPH is a required cofactor for the NADPH oxidase to produce reactive oxygen metabolites, an important microbicidal tool in host defense. p21-Activated kinases (Paks) are regulated by the GTPases Rac and Cdc42 and control actin dynamics and phosphorylation of the oxidase component p47phox . Here we report the interaction of Pak with phosphoglycerate mutase (PGAM)-B, an enzyme of the glycolytic pathway. Activated Pak1 inhibits glycolysis by association of its catalytic domain with PGAM-B and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing PGAM activity. Leukocyte activation through chemoattractant receptors leads to Pak activation and transient inhibition of endogenous PGAM-B activity. Consistent with these observations, treatment of neutrophils with phosphoglycolic acid, a competitive PGAM-B inhibitor, increases upstream intermediates, thereby amplifying the respiratory burst. These results demonstrate that Rho GTPases regulate the glycolytic pathway through Pak and suggest a link between chemoattractant signaling and metabolic responses to enhance host defense.The invasion of pathogens presents an acute challenge to the host organism, which requires an immediate defensive response. Innate immune cells, mainly macrophages, neutrophils, Kupffer cells, and microglia, are specialized in the physical destruction of the invading pathogen via phagocytosis and oxidative burst. These activities are elicited by the binding of chemoattractants including bacterial-derived formylated peptides (formyl-Met-Leu-Phe) to G protein-coupled receptors on the cell surface. The chemotactic stimulus leads to activation of the low molecular weight GTP-binding proteins Rac and Cdc42 and their downstream mediators p21-activated kinases (Paks) 1 (1, 2). Rac and Pak signaling is essential in cytoskeletal reorganization including membrane ruffling and formation of filopodia and lamellipodia, thus enabling cell motility during the chemotactic response (3-5), as well as in pathogen-induced respiratory burst activity mediated by a Rac2-regulated multimeric NADPH oxidase enzyme (2, 6). The NADPH oxidase converts molecular oxygen to superoxide anion by electron transport from NADPH, a process that involves translocation and association of active Rac, p67phox , and phosphorylated p47 phox with membrane-bound cytochrome b 558 (7). Pak participates in this pathway by phosphorylation of several serine residues on p47 phox , which are required for oxidase activity and possibly for assembly of the active oxidase (8). Neutrophils contain at least three Pak isoforms whose fMLF-induced activation kinetics coincide with Rac2 activation, p47 phox phosphorylation, and oxidant production (8, 9).Uptake and destruction of pathogens during phagocytosis are accompanied by simultaneous elevation of glucose transporter 1 translocation, glucose uptake, and oxy...

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Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins

Cited by 72 publications

References 47 publications

Subproteome analysis of the neutrophil cytoskeleton

Subproteome analysis of the neutrophil cytoskeleton

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

A p21-Activated Kinase-controlled Metabolic Switch Up-regulates Phagocyte NADPH Oxidase

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