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First published online 21 September 2004
doi: 10.1242/jcs.01366

Journal of Cell Science 117, 5013-5022 (2004)
Published by The Company of Biologists 2004
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Research Article

A novel partner for Dictyostelium filamin is an {alpha}-helical developmentally regulated protein

Monika Knuth1,*, Nandkumar Khaire1,*, Adam Kuspa2, Si Jie Lu2, Michael Schleicher3 and Angelika A. Noegel,1,{ddagger}

1 Zentrum Biochemie, Institut für Biochemie I, Medizinische Fakultät, Universität zu Köln, 50931 Köln, Germany
2 Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030, USA
3 Institut für Zellbiologie, Ludwig-Maximilians-Universität München, Schillerstrasse 42, 80336 München, Germany

{ddagger} Author for correspondence (e-mail: noegel{at}uni-koeln.de)

Accepted 16 June 2004

The filamins are a family of highly homologous actincrosslinking proteins that stabilize three-dimensional actin networks, link them to membrane proteins and direct intracellular signaling reactions to the actin scaffold through interaction with various binding partners. Here, we describe the first Dictyostelium filamin-interacting protein to be isolated - FIP, a 229.8 kDa protein with two {alpha}-helical coiled coil domains. FIP was identified in a yeast two-hybrid screen using the rod domain of filamin as bait. FIP can also be coimmunoprecipitated with filamin from cellular extracts. Deletion analysis located the interaction domain of FIP to a C-terminal region; by contrast, in filamin rods, repeats 2-4 interacted with the recombinant FIP protein. The 7 kb transcript of FIP is upregulated during early development. Monoclonal antibodies raised against a bacterially expressed FIP polypeptide recognize a 230 kDa developmentally regulated protein in western blots. Immunofluorescence analysis shows a punctate staining pattern in the cytosol and, in cell fractionation experiments, FIP is mainly found in the cytosolic fraction. A fusion protein composed of GFP and the C-terminal part localizes to the plasma membrane and is associated with the cytoskeleton. Expression of the fusion protein affects development and influences the size of the multicellular aggregates and the phototactic behavior of slugs. Thus, FIP might provide a candidate link between the dynamic actin cytoskeleton and signal transduction events during the multicellular stages of Dictyostelium amoebae.

Key words: ABP-120/gelation factor/ddFLN, Yeast two-hybrid system, Coiled coil structure, GFP fusion, Development




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K. S. Kolahi and M. R. K. Mofrad
Molecular Mechanics of Filamin's Rod Domain
Biophys. J., February 1, 2008; 94(3): 1075 - 1083.
[Abstract] [Full Text] [PDF]


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