A common clathrin-mediated machinery co-ordinates cell-cell adhesion and bacterial internalization

Area of Science:

• Cell Biology
• Microbiology
• Infectious Disease

Background:

• Invasive bacterial pathogens frequently target host cell adhesion proteins.
• Listeria monocytogenes invasion involves bacterial InlA protein interacting with host E-cadherin, utilizing clathrin-dependent mechanisms for entry into non-phagocytic cells.

Purpose of the Study:

• To investigate the role of clathrin in the initial stages of cell-cell adhesion.
• To explore the connection between clathrin-mediated internalization and adherens junction (AJ) formation.

Main Methods:

• Observed clathrin phosphorylation and localization during adherens junction formation.
• Investigated clathrin's role in recruiting proteins essential for actin rearrangements during AJ maturation.
• Utilized an InlA/E-cadherin chimera to study cell adhesion and internalization processes.

Main Results:

• Clathrin phosphorylation and transient localization were observed at forming cell-cell contacts.
• Clathrin acts as a scaffold for proteins involved in actin rearrangements during AJ maturation.
• Cells expressing an InlA chimera were internalized by E-cadherin-expressing cells, mimicking bacterial invasion.

Conclusions:

• A common clathrin-mediated machinery may regulate both cell internalization and cell-cell adhesion.
• The relative mobility of interacting partners influences whether clathrin mediates adhesion or internalization.