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  1. Article ; Online: The mammalian endocytic cytoskeleton.

    Abouelezz, Amr / Almeida-Souza, Leonardo

    European journal of cell biology

    2022  Volume 101, Issue 2, Page(s) 151222

    Abstract: Clathrin-mediated endocytosis (CME) is the major route through which cells internalise various substances and recycle membrane components. Via the coordinated action of many proteins, the membrane bends and invaginates to form a vesicle that buds off- ... ...

    Abstract Clathrin-mediated endocytosis (CME) is the major route through which cells internalise various substances and recycle membrane components. Via the coordinated action of many proteins, the membrane bends and invaginates to form a vesicle that buds off-along with its contents-into the cell. The contribution of the actin cytoskeleton to this highly dynamic process in mammalian cells is not well understood. Unlike in yeast, where there is a strict requirement for actin in CME, the significance of the actin cytoskeleton to mammalian CME is variable. However, a growing number of studies have established the actin cytoskeleton as a core component of mammalian CME, and our understanding of its contribution has been increasing at a rapid pace. In this review, we summarise the state-of-the-art regarding our understanding of the endocytic cytoskeleton, its physiological significance, and the questions that remain to be answered.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; Cell Membrane/metabolism ; Clathrin/metabolism ; Cytoskeleton/metabolism ; Endocytosis/physiology ; Mammals/metabolism ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Actins ; Clathrin
    Language English
    Publishing date 2022-04-03
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 391967-5
    ISSN 1618-1298 ; 0070-2463 ; 0171-9335
    ISSN (online) 1618-1298
    ISSN 0070-2463 ; 0171-9335
    DOI 10.1016/j.ejcb.2022.151222
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  2. Article ; Online: A kinder approach to science.

    Almeida-Souza, Leonardo / O'Brien, Lilian

    Trends in cell biology

    2021  Volume 32, Issue 3, Page(s) 177–178

    Abstract: To be kind is to protect and promote the well-being of others. We borrow this definition from the philosophical literature to formulate a simple and powerful principle to make scientific communities and institutions healthier, fairer, and more inclusive. ...

    Abstract To be kind is to protect and promote the well-being of others. We borrow this definition from the philosophical literature to formulate a simple and powerful principle to make scientific communities and institutions healthier, fairer, and more inclusive.
    MeSH term(s) Humans ; Science
    Language English
    Publishing date 2021-12-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2021.11.003
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  3. Article ; Online: Focal adhesions contain three specialized actin nanoscale layers.

    Kumari, Reena / Ven, Katharina / Chastney, Megan / Kokate, Shrikant B / Peränen, Johan / Aaron, Jesse / Kogan, Konstantin / Almeida-Souza, Leonardo / Kremneva, Elena / Poincloux, Renaud / Chew, Teng-Leong / Gunning, Peter W / Ivaska, Johanna / Lappalainen, Pekka

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 2547

    Abstract: Focal adhesions (FAs) connect inner workings of cell to the extracellular matrix to control cell adhesion, migration and mechanosensing. Previous studies demonstrated that FAs contain three vertical layers, which connect extracellular matrix to the ... ...

    Abstract Focal adhesions (FAs) connect inner workings of cell to the extracellular matrix to control cell adhesion, migration and mechanosensing. Previous studies demonstrated that FAs contain three vertical layers, which connect extracellular matrix to the cytoskeleton. By using super-resolution iPALM microscopy, we identify two additional nanoscale layers within FAs, specified by actin filaments bound to tropomyosin isoforms Tpm1.6 and Tpm3.2. The Tpm1.6-actin filaments, beneath the previously identified α-actinin cross-linked actin filaments, appear critical for adhesion maturation and controlled cell motility, whereas the adjacent Tpm3.2-actin filament layer beneath seems to facilitate adhesion disassembly. Mechanistically, Tpm3.2 stabilizes ACF-7/MACF1 and KANK-family proteins at adhesions, and hence targets microtubule plus-ends to FAs to catalyse their disassembly. Tpm3.2 depletion leads to disorganized microtubule network, abnormally stable FAs, and defects in tail retraction during migration. Thus, FAs are composed of distinct actin filament layers, and each may have specific roles in coupling adhesions to the cytoskeleton, or in controlling adhesion dynamics.
    MeSH term(s) Actins/metabolism ; Focal Adhesions/metabolism ; Actin Cytoskeleton/metabolism ; Cytoskeleton/metabolism ; Protein Isoforms/metabolism
    Chemical Substances Actins ; Protein Isoforms
    Language English
    Publishing date 2024-03-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-46868-7
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  4. Article ; Online: Reticular adhesions are assembled at flat clathrin lattices and opposed by active integrin α5β1.

    Hakanpää, Laura / Abouelezz, Amr / Lenaerts, An-Sofie / Culfa, Seyda / Algie, Michael / Bärlund, Jenny / Katajisto, Pekka / McMahon, Harvey / Almeida-Souza, Leonardo

    The Journal of cell biology

    2023  Volume 222, Issue 8

    Abstract: Reticular adhesions (RAs) consist of integrin αvβ5 and harbor flat clathrin lattices (FCLs), long-lasting structures with similar molecular composition as clathrin-mediated endocytosis (CME) carriers. Why FCLs and RAs colocalize is not known. Here, we ... ...

    Abstract Reticular adhesions (RAs) consist of integrin αvβ5 and harbor flat clathrin lattices (FCLs), long-lasting structures with similar molecular composition as clathrin-mediated endocytosis (CME) carriers. Why FCLs and RAs colocalize is not known. Here, we show that RAs are assembled at FCLs in a process controlled by fibronectin (FN) and its receptor, integrin α5β1. We observed that cells on FN-rich matrices displayed fewer FCLs and RAs. CME machinery inhibition abolished RAs and live-cell imaging showed that RA establishment requires FCL coassembly. The inhibitory activity of FN was mediated by the activation of integrin α5β1 at Tensin1-positive fibrillar adhesions. Conventionally, endocytosis disassembles cellular adhesions by internalizing their components. Our results present a novel paradigm in the relationship between these two processes by showing that endocytic proteins can actively function in the assembly of cell adhesions. Furthermore, we show this novel adhesion assembly mechanism is coupled to cell migration via unique crosstalk between cell-matrix adhesions.
    MeSH term(s) Integrin alpha5beta1/genetics ; Integrin alpha5beta1/metabolism ; Clathrin/genetics ; Clathrin/metabolism ; Cell Adhesion/physiology ; Cell Movement ; Endocytosis ; Fibronectins/genetics ; Fibronectins/metabolism ; Focal Adhesions/metabolism
    Chemical Substances Integrin alpha5beta1 ; Clathrin ; Fibronectins
    Language English
    Publishing date 2023-05-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202303107
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  5. Article ; Online: ORP2 couples LDL-cholesterol transport to FAK activation by endosomal cholesterol/PI(4,5)P

    Takahashi, Kohta / Kanerva, Kristiina / Vanharanta, Lauri / Almeida-Souza, Leonardo / Lietha, Daniel / Olkkonen, Vesa M / Ikonen, Elina

    The EMBO journal

    2021  Volume 40, Issue 14, Page(s) e106871

    Abstract: Low-density lipoprotein (LDL)-cholesterol delivery from late endosomes to the plasma membrane regulates focal adhesion dynamics and cell migration, but the mechanisms controlling it are poorly characterized. Here, we employed auxin-inducible rapid ... ...

    Abstract Low-density lipoprotein (LDL)-cholesterol delivery from late endosomes to the plasma membrane regulates focal adhesion dynamics and cell migration, but the mechanisms controlling it are poorly characterized. Here, we employed auxin-inducible rapid degradation of oxysterol-binding protein-related protein 2 (ORP2/OSBPL2) to show that endogenous ORP2 mediates the transfer of LDL-derived cholesterol from late endosomes to focal adhesion kinase (FAK)-/integrin-positive recycling endosomes in human cells. In vitro, cholesterol enhances membrane association of FAK to PI(4,5)P
    MeSH term(s) Biological Transport/physiology ; Cell Adhesion/physiology ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Movement/physiology ; Cholesterol, LDL/metabolism ; Endosomes/metabolism ; Focal Adhesion Kinase 1/metabolism ; Humans ; Phosphatidylinositol Phosphates/metabolism ; Receptors, Steroid/metabolism
    Chemical Substances Cholesterol, LDL ; OSBPL2 protein, human ; Phosphatidylinositol Phosphates ; Receptors, Steroid ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; PTK2 protein, human (EC 2.7.10.2)
    Language English
    Publishing date 2021-06-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2020106871
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  6. Article ; Online: PhD survival guide. Some brief advice for PhD students.

    Almeida-Souza, Leonardo / Baets, Jonathan

    EMBO reports

    2012  Volume 13, Issue 3, Page(s) 189–192

    MeSH term(s) Communication ; Education, Graduate ; Humans ; Publications ; Research ; Students
    Language English
    Publishing date 2012-03-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.1038/embor.2012.15
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  7. Article ; Online: Tyrosyl-tRNA synthetase has a noncanonical function in actin bundling.

    Ermanoska, Biljana / Asselbergh, Bob / Morant, Laura / Petrovic-Erfurth, Maria-Luise / Hosseinibarkooie, Seyyedmohsen / Leitão-Gonçalves, Ricardo / Almeida-Souza, Leonardo / Bervoets, Sven / Sun, Litao / Lee, LaTasha / Atkinson, Derek / Khanghahi, Akram / Tournev, Ivaylo / Callaerts, Patrick / Verstreken, Patrik / Yang, Xiang-Lei / Wirth, Brunhilde / Rodal, Avital A / Timmerman, Vincent /
    Goode, Bruce L / Godenschwege, Tanja A / Jordanova, Albena

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 999

    Abstract: Dominant mutations in tyrosyl-tRNA synthetase (YARS1) and six other tRNA ligases cause Charcot-Marie-Tooth peripheral neuropathy (CMT). Loss of aminoacylation is not required for their pathogenicity, suggesting a gain-of-function disease mechanism. By an ...

    Abstract Dominant mutations in tyrosyl-tRNA synthetase (YARS1) and six other tRNA ligases cause Charcot-Marie-Tooth peripheral neuropathy (CMT). Loss of aminoacylation is not required for their pathogenicity, suggesting a gain-of-function disease mechanism. By an unbiased genetic screen in Drosophila, we link YARS1 dysfunction to actin cytoskeleton organization. Biochemical studies uncover yet unknown actin-bundling property of YARS1 to be enhanced by a CMT mutation, leading to actin disorganization in the Drosophila nervous system, human SH-SY5Y neuroblastoma cells, and patient-derived fibroblasts. Genetic modulation of F-actin organization improves hallmark electrophysiological and morphological features in neurons of flies expressing CMT-causing YARS1 mutations. Similar beneficial effects are observed in flies expressing a neuropathy-causing glycyl-tRNA synthetase. Hence, in this work, we show that YARS1 is an evolutionary-conserved F-actin organizer which links the actin cytoskeleton to tRNA-synthetase-induced neurodegeneration.
    MeSH term(s) Animals ; Humans ; Actins/metabolism ; Charcot-Marie-Tooth Disease/genetics ; Drosophila/genetics ; Glycine-tRNA Ligase/genetics ; Mutation ; RNA, Transfer ; Tyrosine-tRNA Ligase/genetics ; Tyrosine-tRNA Ligase/metabolism ; Cell Line, Tumor
    Chemical Substances Actins ; Glycine-tRNA Ligase (EC 6.1.1.14) ; RNA, Transfer (9014-25-9) ; Tyrosine-tRNA Ligase (EC 6.1.1.1)
    Language English
    Publishing date 2023-03-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-35908-3
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  8. Article ; Online: Multidimensional Dynamics of the Proteome in the Neurodegenerative and Aging Mammalian Brain.

    Andrews, Byron / Murphy, Alan E / Stofella, Michele / Maslen, Sarah / Almeida-Souza, Leonardo / Skehel, J Mark / Skene, Nathan G / Sobott, Frank / Frank, René A W

    Molecular & cellular proteomics : MCP

    2021  Volume 21, Issue 2, Page(s) 100192

    Abstract: The amount of any given protein in the brain is determined by the rates of its synthesis and destruction, which are regulated by different cellular mechanisms. Here, we combine metabolic labeling in live mice with global proteomic profiling to ... ...

    Abstract The amount of any given protein in the brain is determined by the rates of its synthesis and destruction, which are regulated by different cellular mechanisms. Here, we combine metabolic labeling in live mice with global proteomic profiling to simultaneously quantify both the flux and amount of proteins in mouse models of neurodegeneration. In multiple models, protein turnover increases were associated with increasing pathology. This method distinguishes changes in protein expression mediated by synthesis from those mediated by degradation. In the App
    MeSH term(s) Aging ; Alzheimer Disease/metabolism ; Animals ; Brain/metabolism ; Disease Models, Animal ; Mammals/metabolism ; Mice ; Mice, Transgenic ; Proteome/metabolism ; Proteomics/methods
    Chemical Substances Proteome
    Language English
    Publishing date 2021-12-31
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1016/j.mcpro.2021.100192
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  9. Article ; Online: Microtubule dynamics in the peripheral nervous system: A matter of balance.

    Almeida-Souza, Leonardo / Timmerman, Vincent / Janssens, Sophie

    Bioarchitecture

    2012  Volume 1, Issue 6, Page(s) 267–270

    Abstract: The special architecture of neurons in the peripheral nervous system, with axons extending for long distances, represents a major challenge for the intracellular transport system. Two recent studies show that mutations in the small heat shock protein ... ...

    Abstract The special architecture of neurons in the peripheral nervous system, with axons extending for long distances, represents a major challenge for the intracellular transport system. Two recent studies show that mutations in the small heat shock protein HSPB1, which cause an axonal type of Charcot-Marie-Tooth (CMT) neuropathy, affect microtubule dynamics and impede axonal transport. Intriguingly, while at presymptomatic age the neurons in the mutant HSPB1 mouse show a hyperstable microtubule network, at postsymptomatic age, the microtubule network completely lost its stability as reflected by a marked decrease in tubulin acetylation levels. We here propose a model explaining the role of microtubule stabilization and tubulin acetylation in the pathogenesis of HSPB1 mutations.
    Language English
    Publishing date 2012-04-02
    Publishing country United States
    Document type Journal Article
    ISSN 1949-100X
    ISSN (online) 1949-100X
    DOI 10.4161/bioa.1.6.19198
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  10. Article ; Online: Chromatin 3D interaction analysis of the STARD10 locus unveils FCHSD2 as a regulator of insulin secretion.

    Hu, Ming / Cebola, Inês / Carrat, Gaelle / Jiang, Shuying / Nawaz, Sameena / Khamis, Amna / Canouil, Mickaël / Froguel, Philippe / Schulte, Anke / Solimena, Michele / Ibberson, Mark / Marchetti, Piero / Cardenas-Diaz, Fabian L / Gadue, Paul J / Hastoy, Benoit / Almeida-Souza, Leonardo / McMahon, Harvey / Rutter, Guy A

    Cell reports

    2021  Volume 34, Issue 11, Page(s) 108881

    Language English
    Publishing date 2021-03-17
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2021.108881
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