F-actin redistributions at the division site in livingTradescantia stomatal complexes as revealed by microinjection of rhodamine-phalloidin

Cleary, Ann L.

doi:10.1007/bf01272855

Cited by 108 publications

(124 citation statements)

References 46 publications

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“…Actin responses to growth substances in plant cells are not well documented. However, actin filaments in plant cells do change their organization; for example, during the cell cycle (Seagull et al, 1987;Cleary et al, 1992;Zhang et al, 1993), differentiation (Cho and Wick, 1990;Cleary, 1995), interaction with fungus (Kobayashi et al, 1994), and phototropic responses (Meske and Hartmann, 1995;Mineyuki et al, 1995). Although the turnover rate of actin filaments in plant cells has not been determined, interphase microtubule dynamics in plant cells was demonstrated to be faster than that in animal cells (Hush et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Actin Filaments of Guard Cells Are Reorganized in Response to Light and Abscisic Acid

1997

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A set of guard cells surrounding stomata of terrestrial plants function much like sliding doors in a building, opening to allow the CO, uptake required for photosynthesis and closing to reduce water loss during periods of water deficit. Such regulation is initiated by sensing environmental and interna1 stimuli such as light, humidity, CO,, and the plant-stress hormone ABA, and is accomplished by osmotic volume changes of the cells. Previous studies have implicated heterotrimeric G-proteins, the H+ pump, and the movement of various ions regulated by ion channels in these processes (for review, see Assmann, 1993). Thus, guard cells provide an ideal system in which to examine whether other molecules, including cytoskeletal elements, take part in plant signaling and, if so, how they interact with better-characterized ones.Actin filaments and microtubules are dynamic cellular components; they disassemble into their building units,

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Section: Discussionmentioning

confidence: 99%

Actin Filaments of Guard Cells Are Reorganized in Response to Light and Abscisic Acid

1997

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“…However, by metaphase, actin filaments depolymerize in a narrow ring within the wider ring that was once marked by the preprophase band. This constitutes the actin-depleted zone, which represents a negative marker of the future phragmoplast attachment site (Cleary, 1995). Actin is not, however, completely absent from the vicinity of the wider cortical division zone (CDZ) because F-actin is enriched at either side of the actin-depleted zone to form what has been termed 'actin twin peaks' (Sano et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain

Buschmann

Dols

Kopischke

et al. 2015

Journal of Cell Science

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The preprophase band of microtubules performs the crucial function of marking the plane of cell division. Although the preprophase band depolymerises at the onset of mitosis, the division plane is 'memorized' by a cortical division zone to which the phragmoplast is attracted during cytokinesis. Proteins have been discovered that are part of the molecular memory but little is known about how they contribute to phragmoplast guidance. Previously, we found that the microtubule-associated protein AIR9 is found in the cortical division zone at preprophase and returns during cell plate insertion but is absent from the cortex during the intervening mitosis. To identify new components of the preprophase memory, we searched for proteins that interact with AIR9. We detected the kinesin-like calmodulinbinding protein, KCBP, which can be visualized at the predicted cortical site throughout division. A truncation study of KCBP indicates that its MyTH4-FERM domain is required for linking the motor domain to the cortex. These results suggest a mechanism by which minus-end-directed KCBP helps guide the centrifugally expanding phragmoplast to the cortical division site.

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“…Therefore, the actin-based control of cell boundary dynamics is indirect, and the actin cytoskeleton influences cell shape change, in part, by actin and/or myosin-dependent trafficking of hormone transporters (Geldner et al, 2001) and organelles (Prokhnevsky et al, 2008), including those that control the localized delivery of protein complexes and polysaccharides that pattern the cell wall (Leucci et al, 2007;Gutierrez et al, 2009). In this scheme for actin-based growth control, the actin network dynamically rearranges at spatial scales that span from approximately 1-to 10-mm subcellular domains that may locally position organelles (Cleary, 1995;Gibbon et al, 1999;Szymanski et al, 1999) to the more than 100-mm actin bundle networks that operate at the spatial scales of entire cells (Gutierrez et al, 2009;Dyachok et al, 2011). It is clear from the work of several laboratories that the W/SRC and ARP2/3 protein complexes are required to organize cortical actin and actin bundle networks in trichomes (Szymanski et al, 1999;Le et al, 2003;Deeks et al, 2004;Zhang et al, 2005) and cylindrical epidermal cells (Mathur et al, 2003b;Dyachok et al, 2008Dyachok et al, , 2011.…”

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confidence: 99%

The Endoplasmic Reticulum Is a Reservoir for WAVE/SCAR Regulatory Complex Signaling in the Arabidopsis Leaf

et al. 2013

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During plant cell morphogenesis, signal transduction and cytoskeletal dynamics interact to locally organize the cytoplasm and define the geometry of cell expansion. The WAVE/SCAR (for WASP family verprolin homologous/suppressor of cyclic AMP receptor) regulatory complex (W/SRC) is an evolutionarily conserved heteromeric protein complex. Within the plant kingdom W/SRC is a broadly used effector that converts Rho-of-Plants (ROP)/Rac small GTPase signals into Actin-Related Protein2/3 and actin-dependent growth responses. Although the components and biochemistry of the W/SRC pathway are well understood, a basic understanding of how cells partition W/SRC into active and inactive pools is lacking. In this paper, we report that the endoplasmic reticulum (ER) is an important organelle for W/SRC regulation. We determined that a large intracellular pool of the core W/SRC subunit NAP1, like the known positive regulator of W/SRC, the DOCK family guanine nucleotide-exchange factor SPIKE1 (SPK1), localizes to the surface of the ER. The ER-associated NAP1 is inactive because it displays little colocalization with the actin network, and ER localization requires neither activating signals from SPK1 nor a physical association with its W/SRC-binding partner, SRA1. Our results indicate that in Arabidopsis (Arabidopsis thaliana) leaf pavement cells and trichomes, the ER is a reservoir for W/SRC signaling and may have a key role in the early steps of W/SRC assembly and/or activation.

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F-actin redistributions at the division site in livingTradescantia stomatal complexes as revealed by microinjection of rhodamine-phalloidin

Cited by 108 publications

References 46 publications

Actin Filaments of Guard Cells Are Reorganized in Response to Light and Abscisic Acid

Actin Filaments of Guard Cells Are Reorganized in Response to Light and Abscisic Acid

Arabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain

The Endoplasmic Reticulum Is a Reservoir for WAVE/SCAR Regulatory Complex Signaling in the Arabidopsis Leaf

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