Site-specific crosslinking reveals Phosphofructokinase-L inhibition drives self-assembly and attenuation of protein interactions

Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation and inhibition in vitro and in vivo, respectively. Compartmentalized PFKL is hypothesized to modulate metabolic flux consistent with its centr...

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Published inAdvances in biological regulation Vol. 90; p. 100987
Main Authors Sivadas, Athira, McDonald, Eli Fritz, Shuster, Sydney O, Davis, Caitlin M, Plate, Lars
Format Journal Article
LanguageEnglish
Published England 01.12.2023
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Abstract Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation and inhibition in vitro and in vivo, respectively. Compartmentalized PFKL is hypothesized to modulate metabolic flux consistent with its central role as the rate limiting step in glycolysis. PFKL tetramers self-assemble at two interfaces in the monomer (interface 1 and 2), yet how these interfaces contribute to PFKL compartmentalization and drive protein interactions remains unclear. Here, we used site-specific incorporation of noncanonical photocrosslinking amino acids to identify PFKL interactors at interface 1, 2, and the active site. Tandem mass tag-based quantitative interactomics reveals interface 2 as a hotspot for PFKL interactions, particularly with cytoskeletal, glycolytic, and carbohydrate derivative metabolic proteins. Furthermore, PFKL compartmentalization into puncta was observed in human cells using citrate inhibition. Puncta formation attenuated crosslinked protein-protein interactions with the cytoskeleton at interface 2. This result suggests that PFKL compartmentalization sequesters interface 2, but not interface 1, and may modulate associated protein assemblies with the cytoskeleton.
AbstractList Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation and inhibition in vitro and in vivo, respectively. Compartmentalized PFKL is hypothesized to modulate metabolic flux consistent with its central role as the rate limiting step in glycolysis. PFKL tetramers self-assemble at two interfaces in the monomer (interface 1 and 2), yet how these interfaces contribute to PFKL compartmentalization and drive protein interactions remains unclear. Here, we used site-specific incorporation of noncanonical photocrosslinking amino acids to identify PFKL interactors at interface 1, 2, and the active site. Tandem mass tag-based quantitative interactomics reveals interface 2 as a hotspot for PFKL interactions, particularly with cytoskeletal, glycolytic, and carbohydrate derivative metabolic proteins. Furthermore, PFKL compartmentalization into puncta was observed in human cells using citrate inhibition. Puncta formation attenuated crosslinked protein-protein interactions with the cytoskeleton at interface 2. This result suggests that PFKL compartmentalization sequesters interface 2, but not interface 1, and may modulate associated protein assemblies with the cytoskeleton.Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation and inhibition in vitro and in vivo, respectively. Compartmentalized PFKL is hypothesized to modulate metabolic flux consistent with its central role as the rate limiting step in glycolysis. PFKL tetramers self-assemble at two interfaces in the monomer (interface 1 and 2), yet how these interfaces contribute to PFKL compartmentalization and drive protein interactions remains unclear. Here, we used site-specific incorporation of noncanonical photocrosslinking amino acids to identify PFKL interactors at interface 1, 2, and the active site. Tandem mass tag-based quantitative interactomics reveals interface 2 as a hotspot for PFKL interactions, particularly with cytoskeletal, glycolytic, and carbohydrate derivative metabolic proteins. Furthermore, PFKL compartmentalization into puncta was observed in human cells using citrate inhibition. Puncta formation attenuated crosslinked protein-protein interactions with the cytoskeleton at interface 2. This result suggests that PFKL compartmentalization sequesters interface 2, but not interface 1, and may modulate associated protein assemblies with the cytoskeleton.
Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation and inhibition in vitro and in vivo, respectively. Compartmentalized PFKL is hypothesized to modulate metabolic flux consistent with its central role as the rate limiting step in glycolysis. PFKL tetramers self-assemble at two interfaces in the monomer (interface 1 and 2), yet how these interfaces contribute to PFKL compartmentalization and drive protein interactions remains unclear. Here, we used site-specific incorporation of noncanonical photocrosslinking amino acids to identify PFKL interactors at interface 1, 2, and the active site. Tandem mass tag-based quantitative interactomics reveals interface 2 as a hotspot for PFKL interactions, particularly with cytoskeletal, glycolytic, and carbohydrate derivative metabolic proteins. Furthermore, PFKL compartmentalization into puncta was observed in human cells using citrate inhibition. Puncta formation attenuated crosslinked protein-protein interactions with the cytoskeleton at interface 2. This result suggests that PFKL compartmentalization sequesters interface 2, but not interface 1, and may modulate associated protein assemblies with the cytoskeleton.
ArticleNumber 100987
Author Shuster, Sydney O
Plate, Lars
Sivadas, Athira
Davis, Caitlin M
McDonald, Eli Fritz
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  surname: Sivadas
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  organization: Department of Chemistry, Vanderbilt University, Nashville, TN, USA
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  surname: McDonald
  fullname: McDonald, Eli Fritz
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  organization: Department of Chemistry, Vanderbilt University, Nashville, TN, USA; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA; Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: lars.plate@vanderbilt.edu
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Cites_doi 10.1186/1471-2091-14-3
10.1371/journal.pone.0015447
10.1038/s41586-020-1998-1
10.3109/10409238109108700
10.1074/mcp.RA120.002168
10.1016/j.biochi.2010.01.023
10.1007/BF00849191
10.1016/j.apsb.2012.06.002
10.1021/bi020110d
10.1073/pnas.1501373112
10.1042/EBC20180008
10.1083/jcb.99.1.222s
10.1016/j.sbi.2013.06.009
10.1126/science.1084772
10.1016/j.bpj.2020.08.002
10.1038/415141a
10.1021/bi00386a028
10.1016/j.chembiol.2020.07.006
10.1073/pnas.0409741102
10.1016/S1096-7192(03)00117-3
10.1083/jcb.201701084
10.1016/S1096-7192(03)00037-4
10.1093/nar/gky1131
10.1016/j.semcancer.2015.10.002
10.1074/mcp.M114.041012
10.1016/j.xpro.2020.100109
10.1023/B:MCBI.0000009860.86969.72
10.1023/B:MCBI.0000009855.14648.2c
10.7554/eLife.27711
10.1038/s41467-020-14586-5
10.1016/j.celrep.2023.112394
10.1038/nmeth.2019
10.1021/acs.jproteome.1c00168
10.1016/j.chembiol.2017.10.001
10.1038/s41586-018-0201-4
10.1038/nsmb.3407
10.3390/biology3030623
10.1242/jcs.248385
10.1021/acsinfecdis.0c00500
10.1007/s13187-013-0486-9
10.1091/mbc.E21-11-0578
10.1016/j.neuron.2016.03.011
10.1016/j.chembiol.2020.03.004
10.1074/jbc.M117.783050
10.1016/j.cell.2021.07.004
10.1074/mcp.M115.053082
10.1126/science.aay5359
10.1016/j.chembiol.2019.04.001
10.15252/msb.20188792
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References 37781627 - bioRxiv. 2023 Sep 20
El-Bacha (10.1016/j.jbior.2023.100987_bib8) 2003; 79
Futran (10.1016/j.jbior.2023.100987_bib9) 2015; 112
Lynch (10.1016/j.jbior.2023.100987_bib28) 2017; 24
Campanella (10.1016/j.jbior.2023.100987_bib3) 2005; 102
Real-Hohn (10.1016/j.jbior.2023.100987_bib40) 2010; 92
Kemp (10.1016/j.jbior.2023.100987_bib22) 1983; 57
Jang (10.1016/j.jbior.2023.100987_bib19) 2021; 120
Shah (10.1016/j.jbior.2023.100987_bib45) 2020; 27
Hashimoto (10.1016/j.jbior.2023.100987_bib14) 2020; 11
Wu (10.1016/j.jbior.2023.100987_bib51) 2020; 27
Kim (10.1016/j.jbior.2023.100987_bib24) 2023
Ovádi (10.1016/j.jbior.2023.100987_bib36) 2004; 256
Ha (10.1016/j.jbior.2023.100987_bib13) 2023
Plate (10.1016/j.jbior.2023.100987_bib39) 2019; 26
Keilhauer (10.1016/j.jbior.2023.100987_bib21) 2015; 14
Gavin (10.1016/j.jbior.2023.100987_bib10) 2002; 415
Chen (10.1016/j.jbior.2023.100987_bib4) 2020; 1
Ovádi (10.1016/j.jbior.2023.100987_bib37) 2004; 256
Kleiner (10.1016/j.jbior.2023.100987_bib25) 2018; 25
Schindelin (10.1016/j.jbior.2023.100987_bib43) 2012; 9
Kohnhorst (10.1016/j.jbior.2023.100987_bib26) 2017; 292
DeWane (10.1016/j.jbior.2023.100987_bib7) 2021; 134
Ho (10.1016/j.jbior.2023.100987_bib16) 2023; 42
Usenik (10.1016/j.jbior.2023.100987_bib48) 2010; 5
Kemp (10.1016/j.jbior.2023.100987_bib23) 2002; 41
Park (10.1016/j.jbior.2023.100987_bib38) 2020; 578
Kastritis (10.1016/j.jbior.2023.100987_bib20) 2018; 62
Davies (10.1016/j.jbior.2023.100987_bib6) 2020; 6
Guo (10.1016/j.jbior.2023.100987_bib12) 2012; 2
Seidel (10.1016/j.jbior.2023.100987_bib44) 2017; 6
Gomes Alves (10.1016/j.jbior.2023.100987_bib11) 2003; 78
Jang (10.1016/j.jbior.2023.100987_bib18) 2016; 90
Makowski (10.1016/j.jbior.2023.100987_bib29) 2016; 15
Masters (10.1016/j.jbior.2023.100987_bib31) 1984; 99
Stoddard (10.1016/j.jbior.2023.100987_bib46) 2020; 367
Wright (10.1016/j.jbior.2023.100987_bib50) 2021; 20
Roberts (10.1016/j.jbior.2023.100987_bib42) 1987; 26
Masters (10.1016/j.jbior.2023.100987_bib32) 1981; 11
Webb (10.1016/j.jbior.2023.100987_bib49) 2017; 216
McDonald (10.1016/j.jbior.2023.100987_bib33) 2022; 33
Hunkeler (10.1016/j.jbior.2023.100987_bib17) 2018; 558
Chin (10.1016/j.jbior.2023.100987_bib5) 2003; 301
Menard (10.1016/j.jbior.2023.100987_bib34) 2014; 3
Richards (10.1016/j.jbior.2023.100987_bib41) 2021; 17
Akram (10.1016/j.jbior.2023.100987_bib1) 2013; 28
Zhang (10.1016/j.jbior.2023.100987_bib52) 2013; 23
Amara (10.1016/j.jbior.2023.100987_bib2) 2021; 184
Szklarczyk (10.1016/j.jbior.2023.100987_bib47) 2019; 47
Hirschey (10.1016/j.jbior.2023.100987_bib15) 2015; 35
Li (10.1016/j.jbior.2023.100987_bib27) 2021; 20
Masters (10.1016/j.jbior.2023.100987_bib30) 1995
Norris (10.1016/j.jbior.2023.100987_bib35) 2013; 14
References_xml – volume: 14
  start-page: 3
  year: 2013
  ident: 10.1016/j.jbior.2023.100987_bib35
  article-title: Sensor potency of the moonlighting enzyme-decorated cytoskeleton: the cytoskeleton as a metabolic sensor
  publication-title: BMC Biochem.
  doi: 10.1186/1471-2091-14-3
  contributor:
    fullname: Norris
– start-page: 203
  year: 2023
  ident: 10.1016/j.jbior.2023.100987_bib13
  article-title: Carbohydrate metabolism I: glycolysis and the tricarboxylic acid cycle
  contributor:
    fullname: Ha
– volume: 5
  year: 2010
  ident: 10.1016/j.jbior.2023.100987_bib48
  article-title: Evolution of allosteric citrate binding sites on 6-phosphofructo-1-kinase
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0015447
  contributor:
    fullname: Usenik
– volume: 578
  start-page: 621
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib38
  article-title: Mechanical regulation of glycolysis via cytoskeleton architecture
  publication-title: Nature
  doi: 10.1038/s41586-020-1998-1
  contributor:
    fullname: Park
– volume: 11
  start-page: 105
  year: 1981
  ident: 10.1016/j.jbior.2023.100987_bib32
  article-title: Interactions between soluble enzymes and subcellular structur
  publication-title: Crit. Rev. Biochem.
  doi: 10.3109/10409238109108700
  contributor:
    fullname: Masters
– volume: 20
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib50
  article-title: Thyroglobulin interactome profiling defines altered proteostasis topology associated with thyroid dyshormonogenesis
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.RA120.002168
  contributor:
    fullname: Wright
– volume: 92
  start-page: 538
  year: 2010
  ident: 10.1016/j.jbior.2023.100987_bib40
  article-title: Filamentous actin and its associated binding proteins are the stimulatory site for 6-phosphofructo-1-kinase association within the membrane of human erythrocytes
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2010.01.023
  contributor:
    fullname: Real-Hohn
– volume: 57
  start-page: 147
  year: 1983
  ident: 10.1016/j.jbior.2023.100987_bib22
  article-title: Allosteric regulatory properties of muscle phosphofructokinase
  publication-title: Mol. Cell. Biochem.
  doi: 10.1007/BF00849191
  contributor:
    fullname: Kemp
– volume: 2
  start-page: 358
  year: 2012
  ident: 10.1016/j.jbior.2023.100987_bib12
  article-title: Glycolysis in the control of blood glucose homeostasis
  publication-title: Acta Pharm. Sin. B
  doi: 10.1016/j.apsb.2012.06.002
  contributor:
    fullname: Guo
– volume: 41
  start-page: 9426
  year: 2002
  ident: 10.1016/j.jbior.2023.100987_bib23
  article-title: Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase
  publication-title: Biochemistry
  doi: 10.1021/bi020110d
  contributor:
    fullname: Kemp
– volume: 112
  start-page: 8590
  year: 2015
  ident: 10.1016/j.jbior.2023.100987_bib9
  article-title: Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1501373112
  contributor:
    fullname: Futran
– volume: 62
  start-page: 501
  year: 2018
  ident: 10.1016/j.jbior.2023.100987_bib20
  article-title: Enzymatic complexes across scales
  publication-title: Essays Biochem.
  doi: 10.1042/EBC20180008
  contributor:
    fullname: Kastritis
– volume: 99
  start-page: 222s
  year: 1984
  ident: 10.1016/j.jbior.2023.100987_bib31
  article-title: Interactions between glycolytic enzymes and components of the cytomatrix
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.99.1.222s
  contributor:
    fullname: Masters
– volume: 23
  start-page: 581
  year: 2013
  ident: 10.1016/j.jbior.2023.100987_bib52
  article-title: Protein engineering with unnatural amino acids
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2013.06.009
  contributor:
    fullname: Zhang
– volume: 301
  start-page: 964
  year: 2003
  ident: 10.1016/j.jbior.2023.100987_bib5
  article-title: An expanded eukaryotic genetic code
  publication-title: Science
  doi: 10.1126/science.1084772
  contributor:
    fullname: Chin
– year: 2023
  ident: 10.1016/j.jbior.2023.100987_bib24
  article-title: Elexacaftor/VX-445-mediated CFTR interactome remodeling reveals differential correction driven by mutation-specific translational dynamics (preprint)
  publication-title: Cell Biol.
  contributor:
    fullname: Kim
– volume: 120
  start-page: 1170
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib19
  article-title: Phosphofructokinase relocalizes into subcellular compartments with liquid-like properties in vivo
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2020.08.002
  contributor:
    fullname: Jang
– volume: 415
  start-page: 141
  year: 2002
  ident: 10.1016/j.jbior.2023.100987_bib10
  article-title: Functional organization of the yeast proteome by systematic analysis of protein complexes
  publication-title: Nature
  doi: 10.1038/415141a
  contributor:
    fullname: Gavin
– volume: 26
  start-page: 3437
  year: 1987
  ident: 10.1016/j.jbior.2023.100987_bib42
  article-title: Binding of phosphofructokinase to filamentous actin
  publication-title: Biochemistry
  doi: 10.1021/bi00386a028
  contributor:
    fullname: Roberts
– volume: 27
  start-page: 1308
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib45
  article-title: Site-specific incorporation of genetically encoded photo-crosslinkers locates the heteromeric interface of a GPCR complex in living cells
  publication-title: Cell Chem. Biol.
  doi: 10.1016/j.chembiol.2020.07.006
  contributor:
    fullname: Shah
– volume: 102
  start-page: 2402
  year: 2005
  ident: 10.1016/j.jbior.2023.100987_bib3
  article-title: Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0409741102
  contributor:
    fullname: Campanella
– volume: 79
  start-page: 294
  year: 2003
  ident: 10.1016/j.jbior.2023.100987_bib8
  article-title: Cellular distribution of phosphofructokinase activity and implications to metabolic regulation in human breast cancer
  publication-title: Mol. Genet. Metabol.
  doi: 10.1016/S1096-7192(03)00117-3
  contributor:
    fullname: El-Bacha
– volume: 216
  start-page: 2305
  year: 2017
  ident: 10.1016/j.jbior.2023.100987_bib49
  article-title: The glycolytic enzyme phosphofructokinase-1 assembles into filaments
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201701084
  contributor:
    fullname: Webb
– volume: 78
  start-page: 302
  year: 2003
  ident: 10.1016/j.jbior.2023.100987_bib11
  article-title: Epinephrine modulates cellular distribution of muscle phosphofructokinase
  publication-title: Mol. Genet. Metabol.
  doi: 10.1016/S1096-7192(03)00037-4
  contributor:
    fullname: Gomes Alves
– volume: 47
  start-page: D607
  year: 2019
  ident: 10.1016/j.jbior.2023.100987_bib47
  article-title: STRING v11: protein–protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky1131
  contributor:
    fullname: Szklarczyk
– volume: 35
  start-page: S129
  year: 2015
  ident: 10.1016/j.jbior.2023.100987_bib15
  article-title: Dysregulated metabolism contributes to oncogenesis
  publication-title: Semin. Cancer Biol.
  doi: 10.1016/j.semcancer.2015.10.002
  contributor:
    fullname: Hirschey
– volume: 14
  start-page: 120
  year: 2015
  ident: 10.1016/j.jbior.2023.100987_bib21
  article-title: Accurate protein complex retrieval by affinity enrichment mass spectrometry (AE-MS) rather than affinity purification mass spectrometry (AP-MS)
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.M114.041012
  contributor:
    fullname: Keilhauer
– volume: 1
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib4
  article-title: Protocol for site-specific photo-crosslinking proteomics to identify protein-protein interactions in mammalian cells
  publication-title: STAR Protoc
  doi: 10.1016/j.xpro.2020.100109
  contributor:
    fullname: Chen
– volume: 256
  start-page: 83
  year: 2004
  ident: 10.1016/j.jbior.2023.100987_bib36
  article-title: Functional aspects of cellular microcompartmentation in the development of neurodegeneration: mutation induced aberrant protein-protein associations
  publication-title: Mol. Cell. Biochem.
  doi: 10.1023/B:MCBI.0000009860.86969.72
  contributor:
    fullname: Ovádi
– volume: 256
  start-page: 5
  year: 2004
  ident: 10.1016/j.jbior.2023.100987_bib37
  article-title: On the origin of intracellular compartmentation and organized metabolic systems
  publication-title: Mol. Cell. Biochem.
  doi: 10.1023/B:MCBI.0000009855.14648.2c
  contributor:
    fullname: Ovádi
– volume: 6
  year: 2017
  ident: 10.1016/j.jbior.2023.100987_bib44
  article-title: Structural insight into the activation of a class B G-protein-coupled receptor by peptide hormones in live human cells
  publication-title: Elife
  doi: 10.7554/eLife.27711
  contributor:
    fullname: Seidel
– volume: 11
  start-page: 806
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib14
  article-title: Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-020-14586-5
  contributor:
    fullname: Hashimoto
– volume: 42
  year: 2023
  ident: 10.1016/j.jbior.2023.100987_bib16
  article-title: A plasma membrane-associated glycolytic metabolon is functionally coupled to KATP channels in pancreatic α and β cells from humans and mice
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2023.112394
  contributor:
    fullname: Ho
– volume: 9
  start-page: 676
  year: 2012
  ident: 10.1016/j.jbior.2023.100987_bib43
  article-title: Fiji: an open-source platform for biological-image analysis
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2019
  contributor:
    fullname: Schindelin
– volume: 20
  start-page: 2964
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib27
  article-title: TMTpro-18plex: the expanded and complete set of TMTpro reagents for sample multiplexing
  publication-title: J. Proteome Res.
  doi: 10.1021/acs.jproteome.1c00168
  contributor:
    fullname: Li
– volume: 25
  start-page: 110
  year: 2018
  ident: 10.1016/j.jbior.2023.100987_bib25
  article-title: A chemical proteomics approach to reveal direct protein-protein interactions in living cells
  publication-title: Cell Chem. Biol.
  doi: 10.1016/j.chembiol.2017.10.001
  contributor:
    fullname: Kleiner
– volume: 558
  start-page: 470
  year: 2018
  ident: 10.1016/j.jbior.2023.100987_bib17
  article-title: Structural basis for regulation of human acetyl-CoA carboxylase
  publication-title: Nature
  doi: 10.1038/s41586-018-0201-4
  contributor:
    fullname: Hunkeler
– volume: 24
  start-page: 507
  year: 2017
  ident: 10.1016/j.jbior.2023.100987_bib28
  article-title: Human CTP synthase filament structure reveals the active enzyme conformation
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3407
  contributor:
    fullname: Lynch
– volume: 3
  start-page: 623
  year: 2014
  ident: 10.1016/j.jbior.2023.100987_bib34
  article-title: The structural and functional coordination of glycolytic enzymes in muscle: evidence of a metabolon?
  publication-title: Biology
  doi: 10.3390/biology3030623
  contributor:
    fullname: Menard
– volume: 134
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib7
  article-title: Fueling the cytoskeleton – links between cell metabolism and actin remodeling
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.248385
  contributor:
    fullname: DeWane
– volume: 6
  start-page: 3174
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib6
  article-title: Comparative multiplexed interactomics of SARS-CoV-2 and homologous coronavirus nonstructural proteins identifies unique and shared host-cell dependencies
  publication-title: ACS Infect. Dis.
  doi: 10.1021/acsinfecdis.0c00500
  contributor:
    fullname: Davies
– volume: 28
  start-page: 454
  year: 2013
  ident: 10.1016/j.jbior.2023.100987_bib1
  article-title: Mini-review on glycolysis and cancer
  publication-title: J. Cancer Educ.
  doi: 10.1007/s13187-013-0486-9
  contributor:
    fullname: Akram
– volume: 33
  start-page: ar62
  year: 2022
  ident: 10.1016/j.jbior.2023.100987_bib33
  article-title: Distinct proteostasis states drive pharmacologic chaperone susceptibility for cystic fibrosis transmembrane conductance regulator misfolding mutants
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.E21-11-0578
  contributor:
    fullname: McDonald
– volume: 90
  start-page: 278
  year: 2016
  ident: 10.1016/j.jbior.2023.100987_bib18
  article-title: Glycolytic enzymes localize to synapses under energy stress to support synaptic function
  publication-title: Neuron
  doi: 10.1016/j.neuron.2016.03.011
  contributor:
    fullname: Jang
– volume: 27
  start-page: 571
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib51
  article-title: Site-specific photo-crosslinking proteomics reveal regulation of IFITM3 trafficking and turnover by VCP/p97 ATPase
  publication-title: Cell Chem. Biol.
  doi: 10.1016/j.chembiol.2020.03.004
  contributor:
    fullname: Wu
– volume: 292
  start-page: 9191
  year: 2017
  ident: 10.1016/j.jbior.2023.100987_bib26
  article-title: Identification of a multienzyme complex for glucose metabolism in living cells
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M117.783050
  contributor:
    fullname: Kohnhorst
– start-page: 1
  year: 1995
  ident: 10.1016/j.jbior.2023.100987_bib30
  article-title: On the role of the cytoskeleton in metabolic compartmentation
  contributor:
    fullname: Masters
– volume: 184
  start-page: 4480
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib2
  article-title: Selective activation of PFKL suppresses the phagocytic oxidative burst
  publication-title: Cell
  doi: 10.1016/j.cell.2021.07.004
  contributor:
    fullname: Amara
– volume: 15
  start-page: 854
  year: 2016
  ident: 10.1016/j.jbior.2023.100987_bib29
  article-title: Cross-linking immunoprecipitation-MS (xIP-MS): topological analysis of chromatin-associated protein complexes using single affinity purification
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.M115.053082
  contributor:
    fullname: Makowski
– volume: 367
  start-page: 1039
  year: 2020
  ident: 10.1016/j.jbior.2023.100987_bib46
  article-title: Polymerization in the actin ATPase clan regulates hexokinase activity in yeast
  publication-title: Science
  doi: 10.1126/science.aay5359
  contributor:
    fullname: Stoddard
– volume: 26
  start-page: 913
  year: 2019
  ident: 10.1016/j.jbior.2023.100987_bib39
  article-title: Quantitative interactome proteomics reveals a molecular basis for ATF6-dependent regulation of a destabilized amyloidogenic protein
  publication-title: Cell Chem. Biol.
  doi: 10.1016/j.chembiol.2019.04.001
  contributor:
    fullname: Plate
– volume: 17
  year: 2021
  ident: 10.1016/j.jbior.2023.100987_bib41
  article-title: Mass spectrometry‐based protein–protein interaction networks for the study of human diseases
  publication-title: Mol. Syst. Biol.
  doi: 10.15252/msb.20188792
  contributor:
    fullname: Richards
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Snippet Phosphofructokinase is the central enzyme in glycolysis and constitutes a highly regulated step. The liver isoform (PFKL) compartmentalizes during activation...
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Title Site-specific crosslinking reveals Phosphofructokinase-L inhibition drives self-assembly and attenuation of protein interactions
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