@article{MTMT:34736450, title = {Mitochondria in disease: changes in shapes and dynamics}, url = {https://m2.mtmt.hu/api/publication/34736450}, author = {Jenkins, B.C. and Neikirk, K. and Katti, P. and Claypool, S.M. and Kirabo, A. and McReynolds, M.R. and Hinton, A. Jr.}, doi = {10.1016/j.tibs.2024.01.011}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34736450}, issn = {0968-0004}, abstract = {Mitochondrial structure often determines the function of these highly dynamic, multifunctional, eukaryotic organelles, which are essential for maintaining cellular health. The dynamic nature of mitochondria is apparent in descriptions of different mitochondrial shapes [e.g., donuts, megamitochondria (MGs), and nanotunnels] and crista dynamics. This review explores the significance of dynamic alterations in mitochondrial morphology and regulators of mitochondrial and cristae shape. We focus on studies across tissue types and also describe new microscopy techniques for detecting mitochondrial morphologies both in vivo and in vitro that can improve understanding of mitochondrial structure. We highlight the potential therapeutic benefits of regulating mitochondrial morphology and discuss prospective avenues to restore mitochondrial bioenergetics to manage diseases related to mitochondrial dysfunction. © 2024 The Authors}, keywords = {PHARMACOLOGY; MOUSE; MICROSCOPY; MICROSCOPY; DYNAMICS; review; human; MORPHOLOGY; Therapy; nonhuman; diagnosis; in vitro study; mitochondrion; energy metabolism; electric potential; Bioenergy; eukaryote; cell organelle; CONTACT SITES; Clinical diagnostics; Cristae dynamics; mitochondrial morphology; mitochondrial shapes}, year = {2024}, eissn = {1362-4326} } @article{MTMT:34591141, title = {Taking Me away: the function of phosphorylation on histone lysine demethylases}, url = {https://m2.mtmt.hu/api/publication/34591141}, author = {Karakatsanis, N.M. and Hamey, J.J. and Wilkins, M.R.}, doi = {10.1016/j.tibs.2023.12.004}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34591141}, issn = {0968-0004}, year = {2024}, eissn = {1362-4326} } @article{MTMT:34675804, title = {Causes and consequences of DNA single-strand breaks}, url = {https://m2.mtmt.hu/api/publication/34675804}, author = {Caldecott, Keith W.}, doi = {10.1016/j.tibs.2023.11.001}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, volume = {49}, unique-id = {34675804}, issn = {0968-0004}, year = {2024}, eissn = {1362-4326}, pages = {68-78} } @article{MTMT:34661073, title = {UFMylation: a ubiquitin-like modification}, url = {https://m2.mtmt.hu/api/publication/34661073}, author = {Zhou, Xingchen and Mahdizadeh, Sayyed J. and Le Gallo, Matthieu and Eriksson, Leif A. and Chevet, Eric and Lafont, Elodie}, doi = {10.1016/j.tibs.2023.10.004}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, volume = {49}, unique-id = {34661073}, issn = {0968-0004}, year = {2024}, eissn = {1362-4326}, pages = {52-67}, orcid-numbers = {Eriksson, Leif A./0000-0001-5654-3109; Lafont, Elodie/0000-0003-1978-7491} } @article{MTMT:34647643, title = {Why U matters: detection and functions of pseudouridine modifications in mRNAs}, url = {https://m2.mtmt.hu/api/publication/34647643}, author = {Rodell, Rebecca and Robalin, Nicolas and Martinez, Nicole M.}, doi = {10.1016/j.tibs.2023.10.008}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, volume = {49}, unique-id = {34647643}, issn = {0968-0004}, year = {2024}, eissn = {1362-4326}, pages = {12-27} } @article{MTMT:34604355, title = {Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies}, url = {https://m2.mtmt.hu/api/publication/34604355}, author = {Mistry, Ayush Chandrakant and Chowdhury, Debojyoti and Chakraborty, Soham and Haldar, Shubhasis}, doi = {10.1016/j.tibs.2023.10.009}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, volume = {49}, unique-id = {34604355}, issn = {0968-0004}, abstract = {Molecular chaperones play central roles in sustaining protein homeostasis and preventing protein aggregation. Most studies of these systems have been performed in bulk, providing averaged measurements, though recent singlemolecule approaches have provided an in-depth understanding of the molecular mechanisms of their activities and structural rearrangements during substrate recognition. Chaperone activities have been observed to be substrate specific, with some associated with ATP-dependent structural dynamics and others via interactions with co-chaperones. This Review aims to describe the novel mechanisms of molecular chaperones as revealed by single-molecule approaches, and to provide insights into their functioning and its implications for protein homeostasis and human diseases.}, year = {2024}, eissn = {1362-4326}, pages = {38-51}, orcid-numbers = {Haldar, Shubhasis/0000-0002-4304-5570} } @article{MTMT:34398313, title = {UFMylation: a ubiquitin-like modification}, url = {https://m2.mtmt.hu/api/publication/34398313}, author = {Zhou, X. and Mahdizadeh, S.J. and Le, Gallo M. and Eriksson, L.A. and Chevet, E. and Lafont, E.}, doi = {10.1016/j.tibs.2023.10.004}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34398313}, issn = {0968-0004}, year = {2023}, eissn = {1362-4326} } @article{MTMT:34207188, title = {Multifaceted control of T cell differentiation by STIM1}, url = {https://m2.mtmt.hu/api/publication/34207188}, author = {Gross, S. and Womer, L. and Kappes, D.J. and Soboloff, J.}, doi = {10.1016/j.tibs.2023.08.006}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34207188}, issn = {0968-0004}, year = {2023}, eissn = {1362-4326} } @article{MTMT:34189947, title = {Substrate recognition and transport mechanism of the PIN-FORMED auxin exporters}, url = {https://m2.mtmt.hu/api/publication/34189947}, author = {Ung, K.L. and Schulz, L. and Stokes, D.L. and Hammes, U.Z. and Pedersen, B.P.}, doi = {10.1016/j.tibs.2023.07.006}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34189947}, issn = {0968-0004}, year = {2023}, eissn = {1362-4326} } @article{MTMT:34044094, title = {Substrate and phosphorylation site selection by phosphoprotein phosphatases}, url = {https://m2.mtmt.hu/api/publication/34044094}, author = {Nguyen, H. and Kettenbach, A.N.}, doi = {10.1016/j.tibs.2023.04.004}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, unique-id = {34044094}, issn = {0968-0004}, abstract = {Dynamic protein phosphorylation and dephosphorylation are essential regulatory mechanisms that ensure proper cellular signaling and biological functions. Deregulation of either reaction has been implicated in several human diseases. Here, we focus on the mechanisms that govern the specificity of the dephosphorylation reaction. Most cellular serine/threonine dephosphorylation is catalyzed by 13 highly conserved phosphoprotein phosphatase (PPP) catalytic subunits, which form hundreds of holoenzymes by binding to regulatory and scaffolding subunits. PPP holoenzymes recognize phosphorylation site consensus motifs and interact with short linear motifs (SLiMs) or structural elements distal to the phosphorylation site. We review recent advances in understanding the mechanisms of PPP site-specific dephosphorylation preference and substrate recruitment and highlight examples of their interplay in the regulation of cell division. © 2023 Elsevier Ltd}, keywords = {protein phosphorylation; Mitosis; kinetochore; short linear motif (SLiM); phosphoprotein phosphatases (PPPs); phosphorylation site consensus motifs}, year = {2023}, eissn = {1362-4326} }