Identification of a New Phosphorylation Site in Cardiac Muscle Phosphofructokinase

Harrahy, John J.; Malencik, Dean A.; Zhao, Zhizhuang Joe; Hisaw, Frederick L.; Anderson, Sonia R.

doi:10.1006/bbrc.1997.6677

Cited by 4 publications

(3 citation statements)

References 28 publications

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“…Indeed, K6P regulates the rate of glycolysis in response to cell energy requirements and is likely linked to the mitochondrial ATP synthesis. Phosphorylation of K6P, which seems to occur mainly in its C-terminal regulatory domain50, is involved in the equilibrium between oligomeric forms of the enzyme, in the affinity to substrates and allosteric ligands, in the modulation of the interactions with other proteins, and in its intracellular distribution50515253.…”

Section: Discussionmentioning

confidence: 99%

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

Margenat

Labandera

Gil

et al. 2015

Sci Rep

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The bacterial protein tyrosine phosphatase PtpA is a key virulence factor released by Mycobacterium tuberculosis in the cytosol of infected macrophages. So far only two unrelated macrophage components (VPS33B, GSK3α) have been identified as PtpA substrates. As tyrosine phosphatases are capable of using multiple substrates, we developed an improved methodology to pull down novel PtpA substrates from an enriched P-Y macrophage extract using the mutant PtpA D126A. This methodology reduced non-specific protein interactions allowing the identification of four novel putative PtpA substrates by MALDI-TOF-MS and nano LC-MS: three mitochondrial proteins - the trifunctional enzyme (TFP), the ATP synthase, and the sulfide quinone oxidoreductase - and the cytosolic 6-phosphofructokinase. All these proteins play a relevant role in cell energy metabolism. Using surface plasmon resonance, PtpA was found to bind immunopurified human TFP through its catalytic site since TFP-PtpA association was inhibited by a specific phosphatase inhibitor. Moreover, PtpA wt was capable of dephosphorylating immunopurified human TFP in vitro supporting that TFP may be a bona fide PtpA susbtrate. Overall, these results suggest a novel scenario where PtpA-mediated dephosphorylation may affect pathways involved in cell energy metabolism, particularly the beta oxidation of fatty acids through modulation of TFP activity and/or cell distribution.

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Section: Discussionmentioning

confidence: 99%

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

Margenat

Labandera

Gil

et al. 2015

Sci Rep

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“…Though the liver isoforms of these enzymes apparently are not physiological substrates, the muscle isoform of 6-phospho-fructo-1-kinase is phosphorylated in vivo 408 at a site that is also phosphorylated by PKA in vitro in the presence of troponin C. 409 This same site undergoes cAMPdependent phosphorylation in the heart. 410 The functional consequence of this physiological phosphorylation event remains unresolved.…”

Section: Metabolic Enzymesmentioning

confidence: 99%

Physiological Substrates of cAMP-Dependent Protein Kinase

2001

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“…PFK is phosphorylated by diverse protein kinases (PKAs) at serine, threonine, or tyrosine residues (18–24). Very little is known regarding the sites in which these phosphorylations occur.…”

Section: Regulation Of Muscle Type Pfk By Phosphorylationmentioning

confidence: 99%

Regulation of mammalian muscle type 6‐phosphofructo‐1‐kinase and its implication for the control of the metabolism

et al. 2010

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SummaryPhosphofructokinase (PFK) is a major regulatory glycolytic enzyme and is considered to be the pacemaker of glycolysis. This enzyme presents a puzzling regulatory mechanism that is modulated by a large variety of metabolites, drugs, and intracellular proteins. To date, the mammalian enzyme structure has not yet been resolved. However, it is known that PFK undergoes an intricate oligomerization process, shifting among monomers, dimers, tetramers, and more complex oligomeric structures. The equilibrium between PFK dimers and tetramers is directly correlated with the enzyme regulation, because the dimer exhibits very low catalytic activity, whereas the tetramer is fully active. Several PFK ligands modulate the enzyme, favoring the formation of its dimers or tetramers. The present review integrates recent findings regarding the regulatory aspects of muscle type PFK and discusses their relation to the control of metabolism. IUBMBIUBMB Life, 62(11): 791-796, 2010

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Identification of a New Phosphorylation Site in Cardiac Muscle Phosphofructokinase

Cited by 4 publications

References 28 publications

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

Physiological Substrates of cAMP-Dependent Protein Kinase

Regulation of mammalian muscle type 6‐phosphofructo‐1‐kinase and its implication for the control of the metabolism

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