| Title: |
The Salmonella effector SifA initiates a kinesin-1 and kinesin-3 recruitment process mirroring that mediated by Arl8a and Arl8b |
| Authors: |
Fang, Ziyan; Fallet, Mathieu; Moest, Thomas; Gorvel, Jean-Pierre; Méresse, Stéphane |
| Contributors: |
Centre d'Immunologie de Marseille - Luminy (CIML); Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS); ANR-16-CE15-0023,SalmoTubes,Developpement d'un système de tubulation de membrane in vitro pour tester l'activité des protéine effectrices de Salmonella. Analyse par microcopie à fluorescence et force atomique(2016); ANR-11-LABX-0054,INFORM,Flux d'inFormation et organisation de la membrane(2011) |
| Source: |
ISSN: 0021-9533. |
| Publisher Information: |
CCSD; Company of Biologists |
| Publication Year: |
2022 |
| Collection: |
Aix-Marseille Université: HAL |
| Subject Terms: |
Infection; Effector protein; Lysosome; Molecular motor; Membrane trafficking; Salmonella; [SDV]Life Sciences [q-bio] |
| Description: |
International audience ; When intracellular, pathogenic Salmonella reside in a membrane compartment composed of interconnected vacuoles and tubules, the formation of which depends on the translocation of bacterial effectors into the host cell. Cytoskeletons and their molecular motors are prime targets for these effectors. In this study, we show that the microtubule molecular motor KIF1Bβ (a splice variant of KIF1B), a member of the kinesin-3 family, is a key element for the establishment of the Salmonella replication niche as its absence is detrimental to the stability of bacterial vacuoles and the formation of associated tubules. Kinesin-3 interacts with the Salmonella effector SifA but also with SKIP (also known as PLEKHM2), a host protein complexed to SifA. The interaction with SifA is essential for the recruitment of kinesin-3 on Salmonella vacuoles whereas that with SKIP is incidental. In the non-infectious context, however, the interaction with SKIP is essential for the recruitment and activity of kinesin-3 only on a fraction of the lysosomes. Finally, our results show that, in infected cells, the presence of SifA establishes a kinesin-1 and kinesin-3 recruitment pathway that is analogous to and functions independently of that mediated by the Arl8a and Arl8b GTPases. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1242/jcs.259183 |
| Availability: |
https://amu.hal.science/hal-03952596; https://amu.hal.science/hal-03952596v1/document; https://amu.hal.science/hal-03952596v1/file/jcs259183%20%281%29.pdf; https://doi.org/10.1242/jcs.259183 |
| Rights: |
https://about.hal.science/hal-authorisation-v1/ ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.CEF96837 |
| Database: |
BASE |