title: Orchestration of lymphocyte chemotaxis by mitochondrial dynamics.
abstract: Lymphocyte traffic is required to maintain homeostasis and perform appropriate immunological reactions. To migrate into inflamed tissues, lymphocytes must acquire spatial and functional asymmetries. Mitochondria are highly dynamic organelles that distribute in the cytoplasm to meet specific cellular needs, but whether this is essential to lymphocyte functions is unknown. We show that mitochondria specifically concentrate at the uropod during lymphocyte migration by a process involving rearrangements of their shape. Mitochondrial fission facilitates relocation of the organelles and promotes lymphocyte chemotaxis, whereas mitochondrial fusion inhibits both processes. Our data substantiate a new role for mitochondrial dynamics and suggest that mitochondria redistribution is required to regulate the motor of migrating cells.
authors.affiliation: Venetian Institute of Molecular Medicine, Department of Biomedical Science, University of Padua, 35100 Padua, Italy.
authors.forename: Silvia
authors.initials: S
authors.lastname: Campello
authors.forename: Rosa Ana
authors.initials: RA
authors.lastname: Lacalle
authors.forename: Monica
authors.initials: M
authors.lastname: Bettella
authors.forename: Santos
authors.initials: S
authors.lastname: Mañes
authors.forename: Luca
authors.initials: L
authors.lastname: Scorrano
authors.forename: Antonella
authors.initials: A
authors.lastname: Viola
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000730:Androstadienes / Q000494:pharmacology; D002630:Chemotactic Factors / Q000494:pharmacology; D002634:Chemotaxis, Leukocyte / Q000187:drug effects / Q000502:physiology*; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000235:genetics; D018922:HL-60 Cells; D006801:Humans; D019169:Jurkat Cells; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D008214:Lymphocytes / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D008561:Membrane Fusion / Q000187:drug effects; D053078:Membrane Potential, Mitochondrial / Q000187:drug effects; D026901:Membrane Transport Proteins / Q000235:genetics; D018613:Microscopy, Confocal; D008869:Microtubule-Associated Proteins / Q000235:genetics; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D033681:Mitochondrial Membrane Transport Proteins; D024101:Mitochondrial Proteins / Q000235:genetics; D018994:Myosin Light Chains / Q000378:metabolism; D015739:Nocodazole / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D053140:Organelle Shape / Q000187:drug effects; D037342:Pertussis Toxin / Q000494:pharmacology; D010766:Phosphorylation / Q000187:drug effects; D011753:Pyrones / Q000494:pharmacology; D014162:Transfection; D000077191:Wortmannin
chemical_list: D000730:Androstadienes; D002630:Chemotactic Factors; D008164:Luminescent Proteins; D026901:Membrane Transport Proteins; D008869:Microtubule-Associated Proteins; D033681:Mitochondrial Membrane Transport Proteins; D024101:Mitochondrial Proteins; D018994:Myosin Light Chains; D009840:Oligomycins; D011753:Pyrones; C488322:latrunculeic acid; D000255:Adenosine Triphosphate; D037342:Pertussis Toxin; D020558:GTP Phosphohydrolases; C415198:OPA1 protein, human; C470017:Mfn1 protein, human; C110768:DNM1L protein, human; D034281:Dynamins; D015739:Nocodazole; D000077191:Wortmannin