Joe Carroll

University of Cambridge

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Ian M. Fearnley

Medical Research Council

John E. Walker

Medical Research Council

Shujing Ding

MRC Mitochondrial Biology Unit

David J. Ellar

University of Cambridge

Jiuya He

First Affiliated Hospital of Shihezi University Medical College

Judy Hirst

Medical Research Council

Richard J. Shannon

University of Cambridge

Virginie Rhein

MRC Mitochondrial Biology Unit

Kuang Hu

Moorfields Eye Hospital NHS Foundation Trust

Bazbek Davletov

University of Sheffield

Cooperative Institutions

Candy’s Place

123

University of Nicosia

108

University of Cambridge

Medical Research Council

Centre National de la Recherche Scientifique

Inserm

Harvard University

Weatherford College

National Institutes of Health

MRC Mitochondrial Biology Unit

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Self-assembly of SNARE fusion proteins into star-shaped oligomers

Biochemical Journal (2005)

Colin Rickman Kuang Hu Joe Carroll Bazbek Davletov

Three evolutionarily conserved proteins known as SNAREs (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors) mediate exocytosis from single cell eukaryotes to neurons. Among neuronal SNAREs, syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) reside on the plasma membrane, whereas synaptobrevin resides on synaptic vesicles prior to fusion. The SNARE motifs of the three proteins form a helical bundle which probably drives membrane fusion. Since studies in vivo suggested an importance for multiple SNARE complexes in the fusion process, and models appeared in the literature with large numbers of SNARE bundles executing the fusion process, we analysed the quaternary structure of the full-length native SNARE complexes in detail. By employing a preparative immunoaffinity procedure we isolated all of the SNARE complexes from brain, and have shown by size-exclusion chromatography and negative stain electron microscopy that they exist as approx. 30 nm particles containing, most frequently, 3 or 4 bundles emanating from their centre. Using highly purified, individual, full-length SNAREs we demonstrated that the oligomerization of SNAREs into star-shaped particles with 3 to 4 bundles is an intrinsic property of these proteins and is not dependent on other proteins, as previously hypothesized. The average number of the SNARE bundles in the isolated fusion particles corresponds well with the co-operativity observed in calcium-triggered neuronal exocytosis.

Synaptobrevin

SNARE complex

SNAP25

STX1A

Vesicle fusion

10.1042/bj20041818

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Citations (51)

Correction: Bacillus thuringiensis Cry1Ac toxin interaction with Manduca sexta aminopeptidase N in a model membrane environment (Biochemical Journal (1998) 333 (677-683))

Biochemical Journal (1998)

Matthew A. Cooper Joe Carroll Eric R. Travis D. H. Williams David J. Ellar

Bacillus thuringiensis

Cry1Ac

Source

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Citations (2)

Human METTL20 Methylates Lysine Residues Adjacent to the Recognition Loop of the Electron Transfer Flavoprotein in Mitochondria

Journal of Biological Chemistry (2014)

Virginie Rhein Joe Carroll Jiuya He Shujing Ding Ian M. Fearnley

Protein methylation

Flavoprotein

10.1074/jbc.m114.580464

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Citations (56)

Human METTL12 is a mitochondrial methyltransferase that modifies citrate synthase

FEBS Letters (2017)

Virginie Rhein Joe Carroll Shujing Ding Ian M. Fearnley John E. Walker

The protein methylome in mammalian mitochondria has been little studied until recently. Here, we describe that lysine-368 of human citrate synthase is methylated and that the modifying enzyme, localized in the mitochondrial matrix, is methyltransferase-like protein 12 (METTL12), a member of the family of 7β-strand methyltransferases. Lysine-368 is near the active site of citrate synthase, but removal of methylation has no effect on its activity. In mitochondria, it is possible that some or all of the enzymes of the citric acid cycle, including citrate synthase, are organized in metabolons to facilitate the channelling of substrates between participating enzymes. Thus, possible roles for the methylation of Lys-368 are in controlling substrate channelling itself, or in influencing protein-protein interactions in the metabolon.

10.1002/1873-3468.12649

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Citations (37)

Identification of membrane proteins by tandem mass spectrometry of protein ions

Proceedings of the National Academy of Sciences (2007)

Joe Carroll Matthew C. Altman Ian M. Fearnley John E. Walker

The most common way of identifying proteins in proteomic analyses is to use short segments of sequence ("tags") determined by mass spectrometric analysis of proteolytic fragments. The approach is effective with globular proteins and with membrane proteins with significant polar segments between membrane-spanning alpha-helices, but it is ineffective with other hydrophobic proteins where protease cleavage sites are either infrequent or absent. By developing methods to purify hydrophobic proteins in organic solvents and by fragmenting ions of these proteins by collision induced dissociation with argon, we have shown that partial sequences of many membrane proteins can be deduced easily by manual inspection. The spectra from small proteolipids (1-4 transmembrane alpha-helices) are dominated usually by fragment ions arising from internal amide cleavages, from which internal sequences can be obtained, whereas the spectra from larger membrane proteins (5-18 transmembrane alpha-helices) often contain fragment ions from N- and/or C-terminal parts yielding sequences in those regions. With these techniques, we have, for example, identified an abundant protein of unknown function from inner membranes of mitochondria that to our knowledge has escaped detection in proteomic studies, and we have produced sequences from 10 of 13 proteins encoded in mitochondrial DNA. They include the ND6 subunit of complex I, the last of its 45 subunits to be analyzed. The procedures have the potential to be developed further, for example by using newly introduced methods for protein ion dissociation to induce fragmentation of internal regions of large membrane proteins, which may remain partially folded in the gas phase.

Peripheral membrane protein

10.1073/pnas.0706817104

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Citations (63)

Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase

Proceedings of the National Academy of Sciences (2019)

Joe Carroll Jiuya He Shujing Ding Ian M. Fearnley John E. Walker

Significance Mitochondria generate the cellular fuel, adenosine triphosphate, or ATP, to sustain complex life. Production of ATP depends on the oxidation of energy-rich compounds to produce a chemical potential difference for hydrogen ions (or proton motive force, pmf), across the inner mitochondrial membrane (IMM). Disruption of the IMM, dissipation of the pmf, and cell death occur if the total concentration of calcium inside mitochondria is elevated sufficiently to open a pore in the IMM. It has been proposed that the pore is in the membrane sector of the ATP synthase. Here, we show that five membrane proteins associated with the enzyme’s stator are not involved in the pore, and that the pore persists in the absence of the enzyme complex.

Chemiosmosis

Adenosine triphosphate

Bioenergetics

V-ATPase

10.1073/pnas.1904005116

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Citations (113)

Intramolecular Proteolytic Cleavage ofBacillus thuringiensisCry3A δ-Endotoxin May Facilitate Its Coleopteran Toxicity

Journal of Invertebrate Pathology (1997)

Joe Carroll Daniel Convents Jo Van Damme Annemie Boets Jeroen Van Rie

Leptinotarsa

Bacillus thuringiensis

Colorado potato beetle

Bacillaceae

Cleavage (geology)

10.1006/jipa.1997.4656

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Citations (76)

Author Index

Journal of Biological Chemistry (2013)

Salvatore Adinolfi Alfonso Carlos Mona Al‐Mugotir Claudia Alves Amako Yutaka

10.1016/s0021-9258(20)45186-5

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Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion

Nature (2002)

Kuang Hu Joe Carroll Sergei V. Fedorovich Colin Rickman Andrei Sukhodub

Synaptobrevin

10.1038/415646a

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Citations (197)

Reply to Bernardi: The mitochondrial permeability transition pore and the ATP synthase

Proceedings of the National Academy of Sciences (2020)

John E. Walker Joe Carroll Jiuya He

The mitochondrial permeability transition pore (PTP) is a physiological phenomenon lacking a molecular basis. The phenomenon, described over 40 y ago, is that in response to elevated levels of Ca2+ ions in the mitochondrial matrix a nonspecific channel opens, water enters the mitochondria, their cristae swell, their membranes rupture, terminating ATP synthesis, and cell death by necrosis ensues (1). Pore opening can be inhibited by the binding of cyclosporin A to cyclophilin D, a prolyl cis–trans isomerase in the mitochondrial matrix that interacts with the pore without necessarily being a component. The open pore allows hydrophilic molecules up to a molecular weight of 1,500 Da to … [↵][1]1To whom correspondence may be addressed. Email: walker{at}mrc-mbu.cam.ac.uk. [1]: #xref-corresp-1-1

Cyclophilin

Mitochondrial matrix

10.1073/pnas.1921409117

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Citations (20)