Published March 26, 2007
| Version v1
Journal article
The actin-based motor protein myosin II regulates MHC class II trafficking and BCR-driven antigen presentation.
Contributors
Others:
- Immunité et cancer ; Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)
- Compartimentation et dynamique cellulaires (CDC) ; Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS)
- Department of Dermatology ; Brigham and Women's Hospital [Boston]
- Immunologie des Maladies Infectieuses Allergiques et Autoimmunes ; Université Nice Sophia Antipolis (1965 - 2019) (UNS) ; COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)
- Fondation pour la Recherche Médicale (FRM), Ministère de la Recherche, Association pour la Recherche contre le Cancer, ECOS-CONICYT (project no. C03S01), Universidad Catolica de Chile, Institut Curie, Beca Presidente de la Republica from the Chilean government (Mideplan), Institut National de la Santé et de la Recherche Médicale
Description
Antigen (Ag) capture and presentation onto major histocompatibility complex (MHC) class II molecules by B lymphocytes is mediated by their surface Ag receptor (B cell receptor [BCR]). Therefore, the transport of vesicles that carry MHC class II and BCR-Ag complexes must be coordinated for them to converge for processing. In this study, we identify the actin-associated motor protein myosin II as being essential for this process. Myosin II is activated upon BCR engagement and associates with MHC class II-invariant chain complexes. Myosin II inhibition or depletion compromises the convergence and concentration of MHC class II and BCR-Ag complexes into lysosomes devoted to Ag processing. Accordingly, the formation of MHC class II-peptides and subsequent CD4 T cell activation are impaired in cells lacking myosin II activity. Therefore, myosin II emerges as a key motor protein in BCR-driven Ag processing and presentation.
Additional details
Identifiers
- URL
- https://hal.archives-ouvertes.fr/hal-00316389
- URN
- urn:oai:HAL:hal-00316389v1
Origin repository
- Origin repository
- UNICA