PuSH - Publication Server of Helmholtz Zentrum München: Membrane targeting of the Spir-formin actin nucleator complex requires a sequential handshake of polar interactions.

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Tittel, J.* ; Welz, T.* ; Czogalla, A.* ; Dietrich, S.* ; Samol-Wolf, A.* ; Schulte, M.J.D.* ; Schwille, P.* ; Weidemann, T.* ; Kerkhoff, E.*

Membrane targeting of the Spir-formin actin nucleator complex requires a sequential handshake of polar interactions.

J. Biol. Chem. 290, 6428-6444 (2015)

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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.

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Spir and formin (FMN)-type actin nucleators initiate actin polymerization at vesicular membranes necessary for long range vesicular transport processes. Here we studied in detail the membrane binding properties and protein/protein interactions that govern the assembly of the membrane-associated SpirFMN complex. Using biomimetic membrane models we show that binding of the C-terminal Spir-2 FYVE-type zinc finger involves both the presence of negatively charged lipids and hydrophobic contributions from the turret loop that intrudes the lipid bilayer. In solution, we uncovered a yet unknown intramolecular interaction between the Spir-2 FYVE-type domain and the N-terminal kinase non-catalytic C-lobe domain (KIND) that could not be detected in the membrane-bound state. Interestingly, we found that the intramolecular Spir-2 FYVE/KIND and the trans-regulatory Fmn-2-FSI/Spir-2-KIND interactions are competitive. We therefore characterized co-expressed Spir-2 and Fmn-2 fluorescent protein fusions in living cells by fluorescence cross-correlation spectroscopy. The data corroborate a model according to which Spir-2 exists in two different states, a cytosolic monomeric conformation and a membrane-bound state in which the KIND domain is released and accessible for subsequent Fmn-2 recruitment. This sequence of interactions mechanistically couples membrane binding of Spir to the recruitment of FMN, a pivotal step for initiating actin nucleation at vesicular membranes.

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