IngentaConnect Drebrin particles: components in the ensemble of proteins regulat...

Authors: Peitsch W.K.^{1, 2}; Hofmann I.¹; Prätzel S.¹; Grund C.¹; Kuhn C.¹; Moll I.²; Langbein L.¹; Franke W.W.¹

Source: European Journal of Cell Biology, Volume 80, Number 9, September 2001 , pp. 567-579(13)

Abstract:

Drebrin, an actin-binding 70-kDa protein with an unusually slow SDS-PAGE mobility corresponding to sim 120 kDa, containing a proline-rich, profilin-binding motif, had originally been reported from neuronal cells, but recently has also been found in diverse other kinds of tissues and cell lines. In biochemical analyses of various cells and tissues, employing gel filtration, sucrose gradient centrifugation, immunoprecipitation and -blotting, we have identified distinct states of soluble drebrin: a sim 4S monomer, an 8S, ca. 217-kDa putative trimer, a 13S and a >20S oligomer. In the 8S particles only [³⁵S]methionine-labelled drebrin but no other actin-binding protein has been detected in stoichiometric amounts. By immunofluorescence and immunoelectron microscopy, drebrin-positive material often appeared as “granules” up to 400 nm in diameter, in some cell types clustered near the Golgi apparatus or in lamellipodia, particularly at leading edges, or in dense-packed submembranous masses at tips (acropodia) or ruffles of leading edges, in filopodia and at plaques of adhering junctions. We conclude that these drebrin complexes and drebrin-rich structures allow the build-up and maintenance of high local drebrin concentrations in strategic positions for the regulation of actin filament assembly, thereby contributing to cell motility and morphology, in particular local changes of plasticity and the formation of protrusions.

Keywords: Lamellipodia; filopodia; drebrin; actin-binding proteins; cell motility

Language: English

Document Type: Original article

DOI: 10.1078/0171-9335-00194

Affiliations: 1: Division of Cell Biology, German Cancer Research Center, Heidelberg/Germany 2: Department of Dermatology, University Hospital Eppendorf, University of Hamburg/Germany

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Drebrin particles: components in the ensemble of proteins regulating actin dynamics of lamellipodia and filopodia