Key result
Affinity chromatography and mass spectrometry identified cytoskeleton-associated proteins as interaction partners of FHL2, which co-localised with FHL2 in cell lamellipodia.
FHL2 interacts with cytoskeleton-associated proteins and co-localises with them in cell lamellipodia, supporting its predicted adaptor function.
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No immediate clinical implications; extends FHL2 adaptor hypothesis in cellular models while leaving disease relevance open.
Containing four LIM domains and an N-terminal half LIM domain, FHL2 has been predicted to have an adaptor function in the formation of higher order molecular complexes in the nucleus and the cytoplasm of cells. We expressed recombinant FHL2 in insect cells using the baculovirus system and used it to isolate direct or indirect interaction partners from the cytosolic fraction of fibroblasts by affinity chromatography. These were identified by their peptide mass fingerprints using MALDI-TOF mass spectrometry. Cytoskeleton-associated proteins present among the bound proteins were shown to co-localise with FHL2 in cell lamellipodia by indirect immunofluorescence staining.
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Mourabit et al. (2004) studied this question. Recombinant FHL2 expression and affinity chromatography was evaluated on Identification of direct or indirect interaction partners of FHL2. Affinity chromatography and mass spectrometry identified cytoskeleton-associated proteins as interaction partners of FHL2, which co-localised with FHL2 in cell lamellipodia.
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