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Part of the book series: Developments in Plant and Soil Sciences ((DPSS,volume 89))

Abstract

Profilin has complex effects on the actin cytoskeleton; it can bind to monomeric actin and thereby inhibit polymerization, yet under other conditions it stimulates polymerization. Profilin also binds to polyphosphoinositides and proline-rich proteins which are implicated in signaling events that result in reorganization of the actin cytoskeleton. Plant profilins share many of the same biochemical properties and are structurally similar to non-plant profilins. Microinjection of profilin into plant cells inhibits cytoplasmic streaming, tip growth and cytokinesis through the depolymerization of actin microfilaments. Furthermore, measurements of profilin and actin levels in pollen are consistent with profilin sequestering the bulk of the actin monomer pool. Together these results suggest that profilin serves to sequester actin in plant cells. This simple model is complicated by the fact that there are two functionally-distinct classes of profilin, at least in maize, and in some cells both classes of profilin are expressed in the same cytoplasm. One class of profilin appears to have a high affinity for pollen actin and poly-L-proline, whereas the other class has a 2–4-fold lower affinity for actin and a 2-fold lower affinity for poly-L-proline.

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C. J. Staiger F. Baluška D. Volkmann P. W. Barlow

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© 2000 Springer Science+Business Media Dordrecht

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Gibbon, B.C., Staiger, C.J. (2000). Profilin. In: Staiger, C.J., Baluška, F., Volkmann, D., Barlow, P.W. (eds) Actin: A Dynamic Framework for Multiple Plant Cell Functions. Developments in Plant and Soil Sciences, vol 89. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9460-8_3

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  • DOI: https://doi.org/10.1007/978-94-015-9460-8_3

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