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Cytoskeleton

Reshaping membranes

Nature Reviews Molecular Cell Biology volume 8, pages 342–343 (2007)Cite this article

IRSp53 and MIM are large multidomain proteins that contain an IRSp53/MIM domain (IMD) at their N termini. IMDs share structural homology with BAR domains, which bind and deform lipid membranes in vitro and in vivo. But, in contrast to BAR domains, which are involved in the formation of membrane invaginations, IMDs function in the formation of membrane protrusions.

...IMDs bind to the inner surface of the membrane tubule and therefore promote the formation of plasma-membrane protrusions.

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References

ORIGINAL RESEARCH PAPER

  1. Mattila, P. K. et al. Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism. J. Cell Biol. 26 March 2007 (doi: 10.1083/jcb.200609176)

FURTHER READING

  1. Takenawa, T. & Suetsugu, S. The WASP/WAVE protein network: connecting the membrane to the cytoskeleton. Nature Rev. Mol. Cell Biol. 8, 37–48 (2007)

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  1. Ekat Kritikou
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Kritikou, E. Reshaping membranes. Nat Rev Mol Cell Biol 8, 342–343 (2007). https://doi.org/10.1038/nrm2166

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