title: Actin and pollen tube growth.
abstract: Actin microfilaments (MFs) are essential for the growth of the pollen tube. Although it is well known that MFs, together with myosin, deliver the vesicles required for cell elongation, it is becoming evident that the polymerization of new actin MFs, in a process that is independent of actomyosin-dependent vesicle translocation, is also necessary for cell elongation. Herein we review the recent literature that focuses on this subject, including brief discussions of the actin-binding proteins in pollen, and their possible role in regulating actin MF activity. We promote the view that polymerization of new actin MFs polarizes the cytoplasm at the apex of the tube. This process is regulated in part by the apical calcium gradient and by different actin-binding proteins. For example, profilin binds actin monomers and gives the cell control over the initiation of polymerization. A more recently discovered actin-binding protein, villin, stimulates the formation of unipolar bundles of MFs. Villin may also respond to the apical calcium gradient, fragmenting MFs, and thus locally facilitating actin remodeling. While much remains to be discovered, it is nevertheless apparent that actin MFs play a fundamental role in controlling apical cell growth in pollen tubes.
authors.affiliation: Biology Department, University of Massachusetts, Amherst, MA 01003, USA. lvidali@bio.umass.edu
authors.forename: L
authors.initials: L
authors.lastname: Vidali
authors.forename: P K
authors.initials: PK
authors.lastname: Hepler
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D016764:Cell Polarity; D027762:Lilium / Q000254:growth & development / Q000502:physiology; D008840:Microfilament Proteins / Q000378:metabolism; D018514:Plant Structures / Q000254:growth & development* / Q000378:metabolism / Q000648:ultrastructure; D011058:Pollen
chemical_list: D000199:Actins; D008840:Microfilament Proteins