The Coronin Family of Proteins pp 98-109

Part of the Subcellular Biochemistry book series (SCBI, volume 48)

Evolutionary and Functional Diversity of Coronin Proteins

  • Charles-Peter Xavier
  • Ludwig Eichinger
  • M. Pilar Fernandez
  • Reginald O. Morgan
  • Christoph S. Clemen


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 presented in the first two sections. Their coronins generally bind to F-actin and apparently are involved in proliferation, locomotion and phagocytosis. However, there are so far no studies addressing a putative role of coronin in the virulence of these pathogens. The following section delineates genetic anomalies like the chimeric coronin-fusion products with pelckstrin homology and gelsolin domains that are found in amoeba. Moreover, most nonvertebrate metazoa appear to encode CRN8, CRN9 and CRN7 representatives (for these coronin symbols see Chapter 2), but in e.g., Drosophila melanogaster and Caenorhabditis elegans a CRN9 is missing. The forth section deals with the evolutionary expansion of vertebrate coronins. Experimental data on the F-actin binding CRN2 of Xenopus (Xcoronin) including a Cdc42/Rac interactive binding (CRIB) motif that is also present in other members of the coronin protein family are discussed. Xenopus laevis represents a case for the expansion of the seven vertebrate coronins due to tetraploidization events. Other examples for a change in the number of coronin paralogs are zebrafish and birds, but (coronin) gene duplication events also occurred in unicellular protozoa. The fifth section of this chapter briefly summarizes three different cellular processes in which CRN4/CORO1A is involved, namely actin-binding, superoxide generation and Ca2+-signaling and refers to the largely unexplored mammalian coronins CRN5/CORO2A and CRN6/CORO2B, the latter binding to vinculin. The final section discusses how, by unveiling the aspects of coronin function in organisms reported so far, one can trace a remarkable evolution and diversity in their indivkdual roles anticipating a rather complex and intricate involvement of coronins in a variety of cellular processes.


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Copyright information

© Landes Bioscience and Springer Science+Business Media 2008

Authors and Affiliations

  • Charles-Peter Xavier
    • 3
  • Ludwig Eichinger
    • 3
  • M. Pilar Fernandez
    • 1
    • 2
  • Reginald O. Morgan
    • 1
    • 2
  • Christoph S. Clemen
    • 3
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of OviedoOviedoSpain
  2. 2.Instituto Universitario de Biotecnología de Asturias (IUBA)OviedoSpain
  3. 3.Center for Biochemistry, Medical FacultyUniversity of CologneCologneGermany

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