Regulation of actin dynamics by actin-binding proteins in pollen.
A dynamic network of polymers, the actin cytoskeleton, co-ordinates numerous fundamental cellular processes. In pollen tubes, organelle movements and cytoplasmic streaming, organization of the tip zone, vesicle trafficking, and tip growth have all been linked to actin-based function. Further, during the self-incompatibility response of Papaver rhoeas, destruction of the cytoskeleton is a primary target implicated in the rapid cessation of pollen tube growth and alterations in actin dynamics are associated with the initiation of programmed cell death. Surprisingly, these diverse cellular processes are accomplished with only a small amount of filamentous actin and a huge pool of polymerizable monomers. These observations hint at incredibly fast and complex actin dynamics in pollen. To understand the molecular mechanisms regulating actin dynamics in plant cells, the abundant actin monomer-binding proteins, a major filament nucleator, a family of bundling and severing proteins, and a modulator of growth at the barbed-end of actin filaments have been characterized biochemically. The activities of these proteins are generally consistent with textbook models for actin turnover. For example, the three monomer-binding proteins, profilin, ADF, and CAP, are thought to function synergistically to enhance turnover and the exchange of subunits between monomer and polymer pools. How individual actin filaments behave in living cells, however, remains largely unexplored. Actin dynamics were examined using variable angle epifluorescence microscopy (VAEM) in expanding hypocotyl epidermal cells. Our observations of single filament behaviour are not consistent with filament turnover by treadmilling, but rather represent a novel property called stochastic dynamics. A new model for the dynamic control of actin filament turnover in plant cells is presented.
Staiger
Christopher J
CJ
Department of Biological Sciences and Bindley Bioscience Center, Purdue University, West Lafayette, IN 47907-2064, USA. staiger@purdue.edu
Poulter
Natalie S
NS
Henty
Jessica L
JL
Franklin-Tong
Vernonica E
VE
Blanchoin
Laurent
L
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D007178:Inbreeding; D008840:Microfilament Proteins / Q000378:metabolism*; D008954:Models, Biological; D019441:Plant Epidermis / Q000166:cytology / Q000378:metabolism; D011058:Pollen / Q000166:cytology / Q000378:metabolism*
D000199:Actins; D008840:Microfilament Proteins