The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation

Leslie D. Burtnick, Edward K. Koepf, Jonathan Grimes, E. Yvonne Jones, David I. Stuart, Paul J. McLaughlin, Robert C. Robinson

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229 Citations (Scopus)

Abstract

The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. We propose that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. Domain shifts are proposed in response to Ca2+ as bases for models of how gelsolin acts to sever, cap, or nucleate F-actin filaments. The structure also invites discussion of polyphosphoinositide binding to segment 2 and suggests how mutation at Asp- 187 could initiate a series of events that lead to deposition of amyloid plaques, as observed in victims of familial amyloidosis (Finnish type).

Original languageEnglish
Pages (from-to)661-670
Number of pages10
JournalCell
Volume90
Issue number4
DOIs
Publication statusPublished - Aug 22 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Burtnick, L. D., Koepf, E. K., Grimes, J., Jones, E. Y., Stuart, D. I., McLaughlin, P. J., & Robinson, R. C. (1997). The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation. Cell, 90(4), 661-670. https://doi.org/10.1016/S0092-8674(00)80527-9