TY - JOUR AU - Clarisse, D. AU - Van, Moortel L. AU - Van, Leene C. AU - Gevaert, K. AU - De, Bosscher K. TI - Glucocorticoid receptor signaling: intricacies and therapeutic opportunities JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - In Press PY - 2024 SN - 0968-0004 DO - 10.1016/j.tibs.2024.01.012 UR - https://m2.mtmt.hu/api/publication/34802785 ID - 34802785 N1 - VIB Center for Medical Biotechnology, Ghent, Belgium Department of Biomolecular Medicine, Ghent University, Ghent, Belgium Cancer Research Institute Ghent, Ghent, Belgium Export Date: 21 April 2024 CODEN: TBSCD Correspondence Address: De Bosscher, K.; VIB Center for Medical BiotechnologyBelgium; email: karolien.debosscher@vib-ugent.be LA - English DB - MTMT ER - TY - JOUR AU - Jenkins, B.C. AU - Neikirk, K. AU - Katti, P. AU - Claypool, S.M. AU - Kirabo, A. AU - McReynolds, M.R. AU - Hinton, A. Jr. TI - Mitochondria in disease: changes in shapes and dynamics JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI PY - 2024 SN - 0968-0004 DO - 10.1016/j.tibs.2024.01.011 UR - https://m2.mtmt.hu/api/publication/34736450 ID - 34736450 N1 - Department of Biochemistry and Molecular Biology, The Huck Institute of the Life Sciences, Pennsylvania State University, State College, PA 16801, United States Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232, United States National Heart, Lung and Blood Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, United States Department of Physiology, Mitochondrial Phospholipid Research Center, Department of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, United States Department of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232, United States Vanderbilt Center for Immunobiology, Vanderbilt University Medical Center, Nashville, TN 37232, United States Vanderbilt Institute for Infection, Immunology and Inflammation, Vanderbilt University Medical Center, Nashville, TN 37232, United States Vanderbilt Institute for Global Health, Vanderbilt University Medical Center, Nashville, TN 37232, United States Export Date: 13 March 2024 CODEN: TBSCD Correspondence Address: McReynolds, M.R.; Department of Biochemistry and Molecular Biology, United States; email: mcreynolds@psu.edu Funding details: National Institutes of Health, NIH, R01DK135764, R01GM151746, R01HL144941, R01HL147818, R01HL157584, R01HL165729, R03HL155041, R21TW012635 Funding details: Howard Hughes Medical Institute, HHMI, 1022604, GT15655 Funding details: Burroughs Wellcome Fund, BWF, 1021868.01, 5R25HL106365-12, DK020593 Funding details: Silicon Valley Community Foundation, SVCF Funding details: Vanderbilt Diabetes Research and Training Center, Vanderbilt University Medical Center, VDRTC, 2022-253529 Funding text 1: S.M.C. is funded by National Institutes of Health (NIH) grants R01HL165729 and R01GM151746 . A.K. is funded by NIH grants R01HL147818 , R03HL155041 , R01HL157584 , R01DK135764 , R21TW012635 and R01HL144941 . A.H. is funded by The UNCF/Bristol-Myers Squibb E.E. Just Faculty Fund; Burroughs Wellcome Fund (BWF) Career Award at the Scientific Interface (ID # 1021868.01 ); BWF Ad-hoc Award; NIH Small Research Pilot Subaward to 5R25HL106365-12 from the National Institutes of Health PRIDE Program ( DK020593 ); Vanderbilt Diabetes and Research Training Center Alzheimer’s Disease Pilot & Feasibility Program; and Science Diversity Leadership Grant # 2022-253529 from the Chan Zuckerberg Initiative’s Donor-Advised Fund of the Silicon Valley Community Foundation. M.R.M. is funded by Howard Hughes Medical Institute Hanna H. Gray Fellows Program Faculty Phase Grant # GT15655 and BWF Postdoctoral Diversity Enrichment Program Transition to Faculty Grant # 1022604 . AB - 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 LA - English DB - MTMT ER - TY - JOUR AU - Karakatsanis, N.M. AU - Hamey, J.J. AU - Wilkins, M.R. TI - Taking Me away: the function of phosphorylation on histone lysine demethylases JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI PY - 2024 SN - 0968-0004 DO - 10.1016/j.tibs.2023.12.004 UR - https://m2.mtmt.hu/api/publication/34591141 ID - 34591141 N1 - Export Date: 15 February 2024 CODEN: TBSCD Correspondence Address: Wilkins, M.R.; Systems Biology Initiative, UNSW, Australia; email: m.wilkins@unsw.edu.au LA - English DB - MTMT ER - TY - JOUR AU - Caldecott, Keith W. TI - Causes and consequences of DNA single-strand breaks JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - 49 PY - 2024 IS - 1 SP - 68 EP - 78 PG - 11 SN - 0968-0004 DO - 10.1016/j.tibs.2023.11.001 UR - https://m2.mtmt.hu/api/publication/34675804 ID - 34675804 LA - English DB - MTMT ER - TY - JOUR AU - Zhou, Xingchen AU - Mahdizadeh, Sayyed J. AU - Le Gallo, Matthieu AU - Eriksson, Leif A. AU - Chevet, Eric AU - Lafont, Elodie TI - UFMylation: a ubiquitin-like modification JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - 49 PY - 2024 IS - 1 SP - 52 EP - 67 PG - 16 SN - 0968-0004 DO - 10.1016/j.tibs.2023.10.004 UR - https://m2.mtmt.hu/api/publication/34661073 ID - 34661073 LA - English DB - MTMT ER - TY - JOUR AU - Rodell, Rebecca AU - Robalin, Nicolas AU - Martinez, Nicole M. TI - Why U matters: detection and functions of pseudouridine modifications in mRNAs JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - 49 PY - 2024 IS - 1 SP - 12 EP - 27 PG - 16 SN - 0968-0004 DO - 10.1016/j.tibs.2023.10.008 UR - https://m2.mtmt.hu/api/publication/34647643 ID - 34647643 N1 - Department of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, United States Department of Chemistry, Stanford University, Stanford, CA 94305, United States Department of Developmental Biology, Stanford University, Stanford, CA 94305, United States Sarafan ChEM-H Institute, Stanford University, Stanford, CA 94305, United States Chan Zuckerberg Biohub, San Francisco, CA 94158, United States Export Date: 12 January 2024 CODEN: TBSCD Correspondence Address: Martinez, N.M.; Department of Chemical and Systems Biology, United States; email: nicolemm@stanford.edu LA - English DB - MTMT ER - TY - JOUR AU - Mistry, Ayush Chandrakant AU - Chowdhury, Debojyoti AU - Chakraborty, Soham AU - Haldar, Shubhasis TI - Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI VL - 49 PY - 2024 IS - 1 SP - 38 EP - 51 PG - 14 SN - 0968-0004 DO - 10.1016/j.tibs.2023.10.009 UR - https://m2.mtmt.hu/api/publication/34604355 ID - 34604355 N1 - Export Date: 28 February 2024; CODEN: TBSCD AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Gross, S. AU - Womer, L. AU - Kappes, D.J. AU - Soboloff, J. TI - Multifaceted control of T cell differentiation by STIM1 JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI PY - 2023 SN - 0968-0004 DO - 10.1016/j.tibs.2023.08.006 UR - https://m2.mtmt.hu/api/publication/34207188 ID - 34207188 N1 - Fels Cancer Institute for Personalized Medicine, Lewis Katz School of Medicine at Temple University, Philadelphia, PA 19140, United States Department of Cancer and Cellular Biology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA 19140, United States Fox Chase Cancer Center, Philadelphia, PA 19111, United States Export Date: 19 October 2023 CODEN: TBSCD Correspondence Address: Soboloff, J.; Fels Cancer Institute for Personalized Medicine, United States; email: soboloff@temple.edu LA - English DB - MTMT ER - TY - JOUR AU - Ung, K.L. AU - Schulz, L. AU - Stokes, D.L. AU - Hammes, U.Z. AU - Pedersen, B.P. TI - Substrate recognition and transport mechanism of the PIN-FORMED auxin exporters JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI PY - 2023 SN - 0968-0004 DO - 10.1016/j.tibs.2023.07.006 UR - https://m2.mtmt.hu/api/publication/34189947 ID - 34189947 N1 - Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, 8000, Denmark Plant Systems Biology, School of Life Sciences Weihenstephan, Technical University of Munich, Freising, 85354, Germany Department of Biochemistry and Molecular Pharmacology, New York University School of MedicineNY 10016, United States Export Date: 11 October 2023 CODEN: TBSCD Correspondence Address: Pedersen, B.P.; Department of Molecular Biology and Genetics, Denmark; email: bpp@mbg.au.dk LA - English DB - MTMT ER - TY - JOUR AU - Nguyen, H. AU - Kettenbach, A.N. TI - Substrate and phosphorylation site selection by phosphoprotein phosphatases JF - TRENDS IN BIOCHEMICAL SCIENCES J2 - TRENDS BIOCHEM SCI PY - 2023 SN - 0968-0004 DO - 10.1016/j.tibs.2023.04.004 UR - https://m2.mtmt.hu/api/publication/34044094 ID - 34044094 N1 - Export Date: 3 July 2023 CODEN: TBSCD Correspondence Address: Kettenbach, A.N.; Biochemistry and Cell Biology, United States; email: Arminja.N.Kettenbach@dartmouth.edu Funding details: National Institutes of Health, NIH, R35GM119455 Funding text 1: This work was supported by NIH grant R35GM119455 . We thank Scott Gerber for critically reading the manuscript, Paul Robustelli for discussing IDRs, Wolfgang Peti and Rebecca Page for discussing PP1 inhibitory subunits, and Jakob Nilsson for discussing the role of PPPs substrate specificity. The authors apologize to colleagues whose important contributions to the field were not cited due to space limitations. AB - 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 LA - English DB - MTMT ER -