Article
Biochemistry & Molecular Biology
Hiroto Inagaki, Nao Hosoda, Shin-ichi Hoshino
Summary: Ataxin-2 regulates translation and mRNA stability through cytoplasmic polyadenylation, with DDX6 identified as a positive regulator of this process. The interaction between Ataxin-2 and DDX6 plays a role in regulating the polyadenylation machinery.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Clinical Neurology
Jessica R. Blount, Nikhil C. Patel, Kozeta Libohova, Autumn L. Harris, Wei-Ling Tsou, Alyson Sujkowski, Sokol V. Todi
Summary: Ataxin-3 is a deubiquitinase whose abnormal expansion causes the neurodegenerative disease SCA3. This study suggests that the ubiquitination of Atxn3 may be a regulatory step in the development of SCA3, as it modulates the toxicity and aggregation of the disease-causing protein.
JOURNAL OF THE NEUROLOGICAL SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Mahkameh Abeditashi, Jonasz Jeremiasz Weber, Priscila Pereira Sena, Ana Velic, Maria Kalimeri, Rana Dilara Incebacak Eltemur, Jana Schmidt, Jeannette Huebener-Schmid, Stefan Hauser, Boris Macek, Olaf Riess, Thorsten Schmidt
Summary: The study investigates the role of the nuclear transport receptor KPNB1 in MJD cell models and finds that KPNB1 can modulate the protein levels of ataxin-3 and reduce aggregate load, thereby improving cell viability. Furthermore, the reduction of ataxin-3 induced by KPNB1 appears to be based on protein fragmentation independent of classical MJD-associated proteolytic pathways. These findings suggest KPNB1 as a potential therapeutic target for MJD.
CELLULAR AND MOLECULAR LIFE SCIENCES
(2022)
Article
Neurosciences
Frida Niss, Wajiha Zaidi, Einar Hallberg, Anna-Lena Strom
Summary: The research found that the sequestration of RNA-binding protein FUS in polyQ aggregates may lead to alterations in its RNA regulatory functions, as well as increased DNA damage, playing an important role in the pathology of SCA7.
MOLECULAR AND CELLULAR NEUROSCIENCE
(2021)
Article
Neurosciences
Matthew V. Prifti, Kozeta Libohova, Autumn L. Harris, Wei-Ling Tsou, Sokol V. Todi
Summary: This study investigated the importance of the ubiquitin-binding site 1 (UbS1) on the toxicity of pathogenic Atxn3 in Spinocerebellar Ataxia Type 3 (SCA3). The results showed that mutating UbS1 markedly exacerbated the toxicity of pathogenic Atxn3, and UbS1 regulates the toxicity of Atxn3 by impacting its role in ubiquitin processing.
FRONTIERS IN NEUROSCIENCE
(2023)
Article
Medicine, Research & Experimental
Anna Pluciennik, Yuhong Liu, Elana Molotsky, Gregory B. Marsh, Bedri Ranxhi, Frederick J. Arnold, Sophie St.-Cyr, Beverly Davidson, Naemeh Pourshafie, Andrew P. Lieberman, Wei Gu, Sokol V. Todi, Diane E. Merry
Summary: This study identified the critical role of USP7 in the pathophysiology of spinal and bulbar muscular atrophy (SBMA), showing that reducing USP7 levels can decrease mutant AR aggregation and toxicity. The findings also suggest a similar role for USP7 in other diseases such as spinocerebellar ataxia type 3 (SCA3) and Huntington's disease.
JOURNAL OF CLINICAL INVESTIGATION
(2021)
Article
Biochemistry & Molecular Biology
Xinyu Ma, Caijing Lu, Yuting Chen, Shulin Li, Ningjia Ma, Xuan Tao, Ying Li, Jing Wang, Min Zhou, Yong-Bin Yan, Pilong Li, Kartoosh Heydari, Haiteng Deng, Min Zhang, Cong Yi, Liang Ge
Summary: In this study, the researchers identified CCT2 as an autophagy receptor that regulates the clearance of aggregation-prone proteins in cells and mouse brains. CCT2 selectively associates with aggregation-prone proteins and interacts with autophagosome marker ATG8s. Furthermore, CCT2 specifically promotes the autophagic degradation of solid protein aggregates, independent of other ubiquitin-binding receptors or chaperone-mediated autophagy.
Article
Biochemistry & Molecular Biology
Michael H. M. Gropp, Courtney L. Klaips, F. Ulrich Hartl
Summary: This study investigated the mechanism of aggregate pathology in Huntington's disease using a yeast model, and revealed the role of cellular vulnerability to age-dependent proteostatic decline. The optogenetic aggregation of polyQ protein bypassed the requirement of prion-forming protein for aggregate formation, shedding light on the prion-mediated oligomer formation mechanism.
Article
Biochemical Research Methods
Qi Wan, Sara N. Mouton, Liesbeth M. Veenhoff, Arnold J. Boersma
Summary: This study presents a fluorescence resonance energy transfer (FRET)-based method for monitoring protein self-assembly with continuous and high-throughput capabilities, allowing for the observation of transient intermediate states. The approach utilizes intermolecular FRET between donor and acceptor proteins on the same target protein, providing high sensitivity and straightforward ratiometric imaging. The method was successfully applied to monitor the self-assembly of three different proteins, revealing the regulatory role of the chaperone protein DNAJB6b.
CELL REPORTS METHODS
(2022)
Article
Biochemistry & Molecular Biology
Grace D. Burns, Olivia E. Hilal, Zhihao Sun, Karl-Richard Reutter, G. Michael Preston, Andrew A. Augustine, Jeffrey L. Brodsky, Christopher J. Guerriero
Summary: The study revealed that the use of a proteasome inhibitor was more toxic in yeast cells expressing misfolded membrane proteins. Additionally, yeast lacking the proteasome-specific transcription factor Rpn4p showed similar growth defects. These results underscore the limitations of the proteostasis network in handling stress caused by accumulation of misfolded membrane proteins.
Article
Chemistry, Analytical
Yong-Guang Gao, Le Thi My Le, Xiuhong Zhai, Ivan A. Boldyrev, Shrawan K. Mishra, Alexander Tischer, Toshihiko Murayama, Atsushi Nishida, Julian G. Molotkovsky, Amer Alam, Rhoderick E. Brown
ANALYTICAL CHEMISTRY
(2020)
Review
Cell Biology
Francisco Sarmento Mesquita, F. Gisou van der Goot, Oksana A. Sergeeva
CELLULAR MICROBIOLOGY
(2020)
Article
Cell Biology
Jerome Buergi, Laurence Abrami, Irinka Castanon, Luciano Andres Abriata, Beatrice Kunz, Shixu Emili Yan, Manuel Lera, Sheila Unger, Andrea Superti-Furga, Matteo Dal Peraro, Marcos Gonzalez Gaitan, Francoise Gisou van der Goot
DEVELOPMENTAL CELL
(2020)
Article
Allergy
Bahia Bekhouche, Aurore Tourville, Yamini Ravichandran, Rachida Tacine, Laurence Abrami, Michael Dussiot, Andrea Khau-Dancasius, Olivia Boccara, Meriem Khirat, Marianne Mangeney, Florent Dingli, Damarys Loew, Batiste Boeda, Penelope Jordan, Thierry Jo Molina, Nathalia Bellon, Sylvie Fraitag, Smail Hadj-Rabia, Stephane Blanche, Anne Puel, Sandrine Etienne-Manneville, F. Gisou van der Goot, Jacqueline Cherfils, Olivier Hermine, Jean-Laurent Casanova, Christine Bodemer, Asma Smahi, Jerome Delon
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY
(2020)
Review
Biochemistry & Molecular Biology
Shrawan K. Mishra, Yong-Guang Gao, Xianqiong Zou, Daniel J. Stephenson, Lucy Malinina, Edward H. Hinchcliffe, Charles E. Chalfant, Rhoderick E. Brown
PROGRESS IN LIPID RESEARCH
(2020)
Article
Multidisciplinary Sciences
I. Castanon, J. T. Hannich, L. Abrami, F. Huber, M. Dubois, M. Mueller, F. G. van der Goot, M. Gonzalez-Gaitan
NATURE COMMUNICATIONS
(2020)
Article
Biochemistry & Molecular Biology
Laurence Abrami, Martina Audagnotto, Sylvia Ho, Maria Jose Marcaida, Francisco S. Mesquita, Muhammad U. Anwar, Patrick A. Sandoz, Giulia Fonti, Florence Pojer, Matteo Dal Peraro, F. Gisou van der Goot
Summary: Acyl protein thioesterase APT2 interacts with membranes via its charged beta-tongue, becomes palmitoylated by ZDHHC3/7, and deforms the bilayer to extract substrate acyl chains. APT2 deacylation leads to its membrane release and degradation.
NATURE CHEMICAL BIOLOGY
(2021)
Article
Cell Biology
Matias Blaustein, Estefania Piegari, Camila Martinez Calejman, Antonella Vila, Analia Amante, Maria Victoria Manese, Ari Zeida, Laurence Abrami, Mariela Veggetti, David A. Guertin, F. Gisou van der Goot, Maria Martha Corvi, Alejandro Colman-Lerner
Summary: The study reveals that Akt protein undergoes S-palmitoylation modification, affecting its localization and function. Lack of palmitoylation leads to increased recruitment of Akt to cytoplasmic structures co-localizing with lysosomes during autophagy.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Meng-Jie Zhao, Xiao Yao, Ping Wei, Chen Zhao, Meng Cheng, Dong Zhang, Wen Xue, Wen-Tian He, Weili Xue, Xinxin Zuo, Lei-Lei Jiang, Zhiyuan Luo, Jiaqi Song, Wen-Jie Shu, Han-Ye Yuan, Yi Liang, Hui Sun, Yan Zhou, Yu Zhou, Ling Zheng, Hong-Yu Hu, Jiwu Wang, Hai-Ning Du
Summary: Research has shown that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 can suppress ALS-related proteinopathies and enhance TDP-43's splicing function. This study further demonstrates the importance of TDP-43 O-GlcNAcylation in maintaining neuronal health and function.
Article
Cell Biology
Francisco S. Mesquita, Laurence Abrami, Oksana Sergeeva, Priscilla Turelli, Enya Qing, Beatrice Kunz, Charlene Raclot, Jonathan Paz Montoya, Luciano A. Abriata, Tom Gallagher, Matteo Dal Peraro, Didier Trono, Giovanni D'Angelo, F. Gisou van der Goot
Summary: During SARS-CoV-2 infection, spike protein undergoes lipid modification which controls its biosynthesis and degradation, promoting viral budding. This lipidation leads to the formation of cholesterol and sphingolipid-rich lipid nanodomains in the early Golgi, enhancing virus fusion capacity.
DEVELOPMENTAL CELL
(2021)
Article
Cell Biology
Lei-Lei Jiang, Wen-Liang Guan, Jian-Yang Wang, Shu-Xian Zhang, Hong-Yu Hu
Summary: This study found that the C-terminal fragment TDP-35 of the TDP-43 protein forms inclusions in the cytoplasm and sequesters other RNA-binding proteins (RBPs) through specific RNA binding, leading to dysfunction in target mRNA maturation. The sequestration process is assisted by sequence-specific RNA binding.
JOURNAL OF CELL SCIENCE
(2022)
Article
Biology
Amado Carreras-Sureda, Laurence Abrami, Kim Ji-Hee, Wen-An Wang, Christopher Henry, Maud Frieden, Monica Didier, F. Gisou van der Goot, Nicolas Demaurex
Summary: This study reveals the critical role of ORAI1 channels in the immune synapse, with S-acylation playing a key regulatory role in channel trafficking and function at the synapse. Additionally, ORAI1 S-acylation is found to enhance TCR recruitment to the synapse.
Article
Multidisciplinary Sciences
Gonzalo P. Solis, Arghavan Kazemzadeh, Laurence Abrami, Jana Valnohova, Cecilia Alvarez, F. Gisou van der Goot, Vladimir L. Katanaev
Summary: This study describes the inherent partitioning of G alpha oα subunit between the plasma membrane and Golgi and establishes the SwissKASH assay to probe the substrate specificity of PATs. The findings uncover the remarkable substrate selectivity of PATs in different membrane compartments, which is the basis for PMP compartmentalization.
NATURE COMMUNICATIONS
(2022)
Article
Biochemistry & Molecular Biology
Francisco S. Mesquita, Laurence Abrami, Arthur Samurkas, F. Gisou van Der Goot
Summary: S-acylation is a covalent modification of proteins with fatty acids, allowing dynamic control of protein properties and functions in association with cell membranes. It regulates a substantial portion of the human proteome and has increasingly recognized roles in protein lifespan. Recent advancements have provided new insights into its mechanisms and implications. This review focuses on the importance of S-acylation in the homeostasis, function, and coordination of integral membrane proteins.
Review
Cell Biology
Muhammad U. Anwar, F. Gisou van der Goot
Summary: S-acylation is an important posttranslational modification that regulates cellular processes. This reversible lipid modification affects cellular pathways and physiological processes, and the enzymes and proteins involved in S-acylation are still being discovered and studied.
JOURNAL OF CELL BIOLOGY
(2023)