Most coronin proteins rely on interaction with actin in their functions. Mammalian coronin 7 has not been shown to interact with actin, but rather to bind to the outer side of Golgi complex membranes. Targeting of coronin 7 to Golgi membranes requires the activity of Src kinase and integrity of...

The coronins, first described in Dictyostelium discoideum in 1991, have meanwhile been detected in all eukaryotes except plants. They belong to the superfamily of WD40‑repeat proteins and represent a large family of proteins, which are often involved in cytoskeletal functions. Phylogenetic...

The WD‑repeat‑containing proteins form a very large family that is diverse in both its function and domain structure. Within all these proteins the WD‑repeat domains are thought to have two common features: the domain folds into a beta propeller; and the domains form a platform without any...

What I’d like to do in this chapter is to share with you my recollections from the earliest days of coronin research and then to provide an overview of the still‑developing story of this fascinating family of proteins. In the fall of 1989 I arrived as a postdoc in Guenther Gerisch’s...

The β‑propeller domain is a widespread protein organizational motif. Typically, β‑propeller proteins are encoded by repeated sequences where each repeat unit corresponds to a twisted β‑sheet structural motif; these β‑sheets are arranged in a circle around a central axis to generate...

Coronins have maintained a high degree of conservation over the roughly 800 million years of eukaryotic evolution. From its origins as a single gene in simpler eukaryotes, the mammalian Coronin gene family has expanded to include at least six members (see Chapter 4). Increasing evidence indicates...

Coronins are highly conserved among species, but their function is far from being understood in detail. Here we will introduce members of the family of coronin like proteins from Drosophila melanogaster, Caenorhabditis elegans and the social amoeba Dictyostelium discoideum. Genetic data from D....

This chapter discusses various aspects of coronin phylogeny, structure and function that are of specific interest. Two subfamilies of ancient coronins of unicellular pathogens such as Entamoeba, Trypanosoma, Leishmania and Acanthamoeba as well as of Plasmodium, Babesia, and Trichomonas are...

Coronin is a conserved actin binding protein that promotes cellular processes that rely on rapid remodeling of the actin cytoskeleton, including endocytosis and cell motility. However, the exact mechanism by which coronin contributes to actin dynamics has remained elusive for many years. Here, we...

The WD repeat containing family of coronin proteins is generally referred to as F‑actin‑interacting proteins. While in lower eukaryotes such as Dictyostelium discoideum, the single short coronin protein regulates several F‑actin dependent processes such as motility, phagocytosis and...

The coronin gene family comprises seven vertebrate paralogs and at least five unclassified subfamilies in nonvertebrate metazoa, fungi and protozoa, but no representatives in plants or distant protists. All known members exhibit elevated structural conservation in two unique domains of unknown...

Until recently, structural information about coronins was scarce and the earlier identification of five WD40 repeats gave rise to a structural prediction of a five‑bladed β propeller for the N‑terminal domain of these proteins. More detailed analyses revealed the presence of seven WD40...