Autophagy and the cytoskeleton

  title={Autophagy and the cytoskeleton},
  author={Serge Mostowy and Pascale Cossart},
  pages={209 - 780 - 782}
Actin-based motility is used by various pathogens such as Listeria and Shigella for dissemination within cells and tissues, yet host factors counteracting this process have not been identified. We have recently discovered that infected host cells can prevent actin-based motility of Shigella by compartmentalizing bacteria inside ‘septin cages,’ revealing a novel mechanism of host defense that restricts dissemination. Because bacterial proteins controlling actin-based motility also regulate the… 
Septins as key regulators of actin based processes in bacterial infection
A series of studies are presented revealing that in addition to actin rearrangements the host cell also employs septins, a relatively newly characterized component of the cell cyto-skeleton, to regulate bacterial entry and restrict the dissemination of cytosolic bacteria.
p62 and NDP52 Proteins Target Intracytosolic Shigella and Listeria to Different Autophagy Pathways
A new molecular framework is provided to understand the emerging complexity of autophagy and its ability to achieve specific clearance of intracytosolic bacteria.
Recruitment of the Major Vault Protein by InlK: A Listeria monocytogenes Strategy to Avoid Autophagy
This work shows that InlK is a bona fide virulence factor, poorly expressed in vitro and well expressed in vivo, and that it is anchored to the bacterial surface by sortase A, and reveals that MVP is hijacked by L. monocytogenes in order to counteract the autophagy process.
Survival Strategies of Intracellular Bacterial Pathogens
This chapter reviews the general mechanisms used by bacterial pathogens to gain access to the intracellular habitat and to overcome the specific challenges imposed by the vacuolar and cytosolic lifestyles.
[Functional Characterization of Septin Complexes].
The structural and functional properties of septins and the regulation of their dynamics are reviewed with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytOSkeletons.
Functional Characterization of Septin Complexes
Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments
Host protein phosphorylation during "Shigella flexneri" infection : a phosphoproteomic based systems biology approach
A large subset of co-regulated phosphoproteins were revealed, indicating that both pathogens interfere with similar cellular signaling cascades, and it was shown that the Inositol polyphosphate multikinase IPMK contributes to AKT phosphorylation during infection.
Septin6 and Septin7 GTP Binding Proteins Regulate AP-3- and ESCRT-Dependent Multivesicular Body Biogenesis
It is shown that SEPT6 and SEPT7 complexes bound to F-actin regulate protein sorting during multivesicular body (MVB) biogenesis, and an unsuspected coordination of these sorting machineries during MVB biogenesis is uncovered.
The Pseudomonas aeruginosa N-Acylhomoserine Lactone Quorum Sensing Molecules Target IQGAP1 and Modulate Epithelial Cell Migration
It is proposed that the targeting of IQGAP1 by 3O-C12-HSL can trigger essential changes in the cytoskeleton network and be an essential component in bacterial – human cell communication.
Ubl4A is critical for mitochondrial fusion process under nutrient deprivation stress
The results suggest that Ubl4A promotes the mitochondrial fusion process via Arp2/3 complex during the initial response to nutrient deprivation for cell survival, and could rescue the starvation-induced mitochondrial fragmentation phenotype.