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The Arp2/3 complex has so far been considered to be a single seven-subunit protein complex required for actin nucleation and actin filament polymerization in diverse critical cellular functions including phagocytosis, vesicular trafficking and lamellipodia extension. The Arp2/3 complex is also exploited by bacterial pathogens and viruses during cellular infectious processes. Recent studies suggest that some subunits of the complex are dispensable in specific cellular contexts, pointing to the existence of alternative 'hybrid Arp2/3 complexes' containing other components such as vinculin or ??-actinin, as well as different isoforms or phosphorylation variants of canonical Arp2/3 subunits. Therefore, this diversity should be now considered when assigning specific Arp2/3 assemblies to different actin-dependent cellular processes.

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Over the years, readers have expressed their interest in a collection of the Protein Spotlight articles in book form for themselves, their students, or as a source to refer to. A few months ago, many of our readers reacted very favourably to the possible launch...