Journal
JOURNAL OF CELL BIOLOGY
Volume 183, Issue 7, Pages 1287-1298Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200807023
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Funding
- Fondation pour la Recherche Medicale [INE20041102865]
- Centre National de la Recherche Scientifique
- Ville de Paris
- CNRS
- Institut Curie
- FRM
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Microtubule dynamics are modulated by regulatory proteins that bind to their plus ends (+TIPs [plus end tracking proteins]), such as cytoplasmic linker protein 170 (CLIP-170) or end-binding protein 1 (EB1). We investigated the role of +TIPs during phagocytosis in macrophages. Using RNA interference and dominant-negative approaches, we show that CLIP-170 is specifically required for efficient phagocytosis triggered by alpha M beta 2 integrin/complement receptor activation. This property is not observed for EB1 and EB3. Accordingly, whereas CLIP-170 is dynamically enriched at the site of phagocytosis, EB1 is not. Furthermore, we observe that CLIP-170 controls the recruitment of the formin mDia1, an actin-nucleating protein, at the onset of phagocytosis and thereby controls actin polymerization events that are essential for phagocytosis. CLIP-170 directly interacts with the formin homology 2 domain of mDia1. The interaction between CLIP-170 and mDia1 is negatively regulated during alpha M beta 2-mediated phagocytosis. Our results unravel a new microtubule/actin cooperation that involves CLIP-170 and mDia1 and that functions downstream of alpha M beta 2 integrins.
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