Interaction between HERC1 and M2‐type pyruvate kinase

Garcia-Gonzalo, Francesc R.; Cruz, Cristina D.; Muñoz, Purificacı́on; Mazurek, Sybille; Eigenbrodt, Erich; Ventura, Francesc; Bartrons, Ramón; Rosa, José Luís

doi:10.1016/s0014-5793(03)00205-9

Cited by 38 publications

(34 citation statements)

References 28 publications

(48 reference statements)

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“…Endogenous pyruvate kinase and clathrin proteins were shown to display punctate cytosolic and perinuclear staining when their subcellular localization was analyzed by confocal microscopy. This presumably indicates that both proteins are associated with membranous compartments (Wasiak et al, 2002;Garcia-Gonzalo et al, 2003) and is in agreement with the data reporting pyruvate kinase activation by PS-containing liposomes (Dabrowska and Czapinska, 1990). LPA might thus also play a role in tethering pyruvate kinase to intracellular membrane structures.…”

Section: Discussionsupporting

confidence: 87%

“…Whereas pyruvate kinase appeared to be distributed uniformly in the cytoplasm with occasional enrichment in particular areas, clathrin showed enrichment in the perinuclear area, in addition to a characteristic dot-like distribution in the cytoplasm. This punctate staining may suggest that these proteins interact with intracellular membranous structures (Wasiak et al, 2002;Garcia-Gonzalo et al, 2003). Of note, superposition of both images showed a partial overlap in distinct areas of the cell, particularly in the perinuclear region, with occasional co-localization in isolated cytoplasmic membranous compartments.…”

Section: Clathrin and Pyruvate Kinase Partly Co-localize In Mcf-7 Cellsmentioning

confidence: 95%

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Detection of Serum Lysophosphatidic Acids Using Affinity Binding and Surface Enhanced Laser Deorption/Ionization (SELDI) Time of Flight Mass Spectrometry

Mills¹

2006

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Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. REPORT DATE (DD-MM-YYYY) 01-04-2006 REPORT TYPE SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel CommandFort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S) DISTRIBUTION / AVAILABILITY STATEMENTApproved for Public Release; Distribution Unlimited SUPPLEMENTARY NOTESOriginal contains color plates: All DTIC reproductions will be in black and white. ABSTRACTWe proposed to apply novel technologies to the development of an approach suitable to detect plasma and serum lipid levels for screening for ovarian cancer in high and low risk women. The first of these is a novel approach to the development of antibodies, which will recognize specific phospholipids and lysophospholipids present in ovarian cancer patients and the second of these is SELDI tof mass spectroscopy. These two technologies will be merged with powerful computing tools to develop approaches capable of detecting ovarian cancer at an early, curable stage. This approach will further benefit from the expertise of the Mills laboratory (LPA screening, SELDI tof) with that of the Prestwich laboratory (lipid synthesis and antibody development). Results We have completed the studies proposed in the application. We have demonstrated that SELDI mass spectroscopy using nonspecific and affinity matrices has the ability to detect and characterize model lysopholipids including LPC, LPA, S1P and LPS present in plasma and serum. This assay is applicable to relatively large volumes of plasma and serum >2ml. We have also demonstrated that additional mass spectroscopy approaches have a greater degree of sensitivity and specificity when compared to SELDI mass spectroscopy. We proposed to develop and analyze lipid specific antibodies. We have analyzed anti-S1P antibodies as both a theragnostic and a diagnostic using a sensitive ELISA approach. LPA antibodies appear to block the growth of hybridomas due to blocking LPAmediated survival. We thus took an interim step of identifying novel LPA binding proteins as alternative affinity reagents. We also developed novel LPA receptor selective ...

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Section: Discussionsupporting

confidence: 87%

Section: Clathrin and Pyruvate Kinase Partly Co-localize In Mcf-7 Cellsmentioning

confidence: 95%

Detection of Serum Lysophosphatidic Acids Using Affinity Binding and Surface Enhanced Laser Deorption/Ionization (SELDI) Time of Flight Mass Spectrometry

Mills¹

2006

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“…A variety of molecules interact with PKM2 (5,6,8,14,18,19,21,23,24,28,(36)(37)(38)(39)(40)(41)(42)(43)(44)(45)(50)(51)(52)(53)(54)(55)(56)(57)(58)(59)(60)(61)(62)(63)(64)(65). Many of them affect the glycolytic functions of PKM2, which directly regulate the Warburg effect.…”

Section: Nonglycolytic Functions Of Pkm2mentioning

confidence: 99%

Pyruvate Kinase M2: Multiple Faces for Conferring Benefits on Cancer Cells

Tamada

Suematsu

Saya

2012

Clinical Cancer Research

203

197

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The M2 splice isoform of pyruvate kinase (PKM2), an enzyme that catalyzes the later step of glycolysis, is a key regulator of aerobic glycolysis (known as the Warburg effect) in cancer cells. Expression and low enzymatic activity of PKM2 confer on cancer cells the glycolytic phenotype, which promotes rapid energy production and flow of glycolytic intermediates into collateral pathways to synthesize nucleic acids, amino acids, and lipids without the accumulation of reactive oxygen species. PKM2 enzymatic activity has also been shown to be negatively regulated by the interaction with CD44 adhesion molecule, which is a cell surface marker for cancer stem cells. In addition to the glycolytic functions, nonglycolytic functions of PKM2 in cancer cells are of particular interest. PKM2 is induced translocation into the nucleus, where it activates transcription of various genes by interacting with and phosphorylating specific nuclear proteins, endowing cancer cells with a survival and growth advantage. Therefore, inhibitors and activators of PKM2 are well underway to evaluate their anticancer effects and suitability for use as novel therapeutic strategies.

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“…Lv et al [32] recently reported that acetyltransferase P300/CBP-associated factor (PCAF) could catalyze the acetylation of PKM2 at K62 and K305, and acetylation of PKM2 at K305 can promote PKM2 degradation and activating chaperone-mediated autophagocytosis. Garcia-Gonzalo et al [33] found that PKM2 could interact with E3 ubiquitin ligase HERC1, but no ubiquitination of PKM2 was observed. The effect of this interaction merits further investigation.…”

Section: The Structural Features Of Pkm2mentioning

confidence: 99%

Dual roles of PKM2 in cancer metabolism

Wu¹,

Han²

2013

ABBS

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Cancer cells have distinct metabolism that highly depends on glycolysis instead of mitochondrial oxidative phosphorylation alone, known as aerobic glycolysis. Pyruvate kinase (PK), which catalyzes the final step of glycolysis, has emerged as a potential regulator of this metabolic phenotype. Expression of PK type M2 (PKM2) is increased and facilitates lactate production in cancer cells, which determines whether the glucose carbons are degraded to pyruvate and lactate or are channeled into synthetic processes. Modulation of PKM2 catalytic activity also regulates the synthesis of DNA and lipids that are required for cell proliferation. However, the mechanisms by which PKM2 coordinates high-energy requirements with high anabolic activities to support cancer cell proliferation are still not completely understood. This review summarizes the biological characteristics of PKM2 and discusses the dual role in cancer metabolism as well as the potential therapeutic applications. Given its pleiotropic effects on cancer biology, PKM2 represents an attractive target for cancer therapy.

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Interaction between HERC1 and M2‐type pyruvate kinase

Cited by 38 publications

References 28 publications

Detection of Serum Lysophosphatidic Acids Using Affinity Binding and Surface Enhanced Laser Deorption/Ionization (SELDI) Time of Flight Mass Spectrometry

Detection of Serum Lysophosphatidic Acids Using Affinity Binding and Surface Enhanced Laser Deorption/Ionization (SELDI) Time of Flight Mass Spectrometry

Pyruvate Kinase M2: Multiple Faces for Conferring Benefits on Cancer Cells

Dual roles of PKM2 in cancer metabolism

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