How Leiomodin and Tropomodulin use a common fold for different actin assembly functions

Malgorzata Boczkowska, Grzegorz Rebowski, Elena Kremneva, Pekka Lappalainen and Roberto Dominguez ()
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Malgorzata Boczkowska: Perelman School of Medicine, University of Pennsylvania
Grzegorz Rebowski: Perelman School of Medicine, University of Pennsylvania
Elena Kremneva: Institute of Biotechnology, PO Box 56, 00014 University of Helsinki
Pekka Lappalainen: Institute of Biotechnology, PO Box 56, 00014 University of Helsinki
Roberto Dominguez: Perelman School of Medicine, University of Pennsylvania

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations—the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.

Date: 2015
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DOI: 10.1038/ncomms9314

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