The auxin signal for protoplast swelling is perceived by extracellular ABP1

Steffens, Bianka; Feckler, Christian; Palme, Klaus; Christian, May; Böttger, Michael; Lüthen, Hartwig

doi:10.1046/j.1365-313x.2001.01103.x

Cited by 108 publications

(99 citation statements)

References 26 publications

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“…In the same year, it was also proven that ABP1 indeed binds auxin (Jones and Venis, 1989), a result that was later corroborated by the crystal structure determination of ABP1 cocrystallized with auxin (Woo et al 2002). ABP1 antibodies and peptides generated in these biochemical studies were increasingly used for physiological studies in heterologous systems, showing auxin induction of cellular processes such as membrane hyperpolarization (Barbier-Brygoo et al, 1991;Venis et al, 1992), K + fluxes (Thiel et al, 1993), or cell expansion, as evidenced by protoplast swelling assays (Steffens et al, 2001). The importance and function of ABP1 for the plant as a whole remained unclear because attempts to modulate ABP1 protein amounts (particularly, its' downregulation) proved difficult in planta.…”

Section: Timeline Of Abp1 Researchmentioning

confidence: 81%

“…Several lines of evidence support a role for ABP1 in control of cell expansion. Early protoplast swelling assays suggested a role for ABP1 in auxin-mediated cell expansion (Steffens et al, 2001), and overexpression of ABP1 in maize plants confirmed that ABP1 is a positive regulator of cell size (Jones et al, 1998). Accordingly, abp1-null mutant embryos have isodiametric cells that fail to elongate (Chen et al, 2001b), and downregulation of ABP1 in leaf tissues reduces the cell size (Braun et al, 2008).…”

Section: Cell Expansionmentioning

confidence: 90%

“…Additional indirect evidence for ABP1 in the cell wall or at the outer side of the plasma membrane comes from physiological assays that have utilized the full protein, peptides, or antibodies against ABP1 to inhibit or mimic rapid auxin effects such as protoplast swelling or electrophysiological responses (BarbierBrygoo et al, 1991;Venis et al, 1992;Thiel et al, 1993;Steffens et al, 2001). Neither antibody fragments nor peptides can pass the plasma membrane easily by diffusion, thus, if their mode of action is indeed by binding ABP1 or a supposed signaling component, this must take place in the extracellular matrix.…”

Section: In and Out: Abp1 Localizationmentioning

confidence: 99%

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AUXIN BINDING PROTEIN1: The Outsider

2011

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AUXIN BINDING PROTEIN1 (ABP1) is one of the first characterized proteins that bind auxin and has been implied as a receptor for a number of auxin responses. Early studies characterized its auxin binding properties and focused on rapid electrophysiological and cell expansion responses, while subsequent work indicated a role in cell cycle and cell division control. Very recently, ABP1 has been ascribed a role in modulating endocytic events at the plasma membrane and RHO OF PLANTS-mediated cytoskeletal rearrangements during asymmetric cell expansion. The exact molecular function of ABP1 is still unresolved, but its main activity apparently lies in influencing events at the plasma membrane. This review aims to connect the novel findings with the more classical literature on ABP1 and to point out the many open questions that still separate us from a comprehensive model of ABP1 action, almost 40 years after the first reports of its existence.

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Section: Timeline Of Abp1 Researchmentioning

confidence: 81%

Section: Cell Expansionmentioning

confidence: 90%

Section: In and Out: Abp1 Localizationmentioning

confidence: 99%

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AUXIN BINDING PROTEIN1: The Outsider

2011

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“…3). In addition ABP1 was shown to mediate the auxin-induced enlargement (or swelling) of protoplasts of maize coleoptiles and Arabidopsis hypocotyls (Steffens et al 2001). Analysis of the swelling response of protoplasts of pea stem epidermal cells revealed a biphasic dose response curve to IAA, one phase being dependent on ABP1 but not the other, suggesting that at least in these epidermal cells another pathway is involved (Yamagami et al 2004).…”

Section: Abp1 and Cell Expansionmentioning

confidence: 97%

Cellular Responses to Auxin: Division versus Expansion

Perrot‐Rechenmann¹

2010

Cold Spring Harbor Perspectives in Biology

480

347

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The phytohormone auxin is a major regulator of plant growth and development. Many aspects of these processes depend on the multiple controls exerted by auxin on cell division and cell expansion. The detailed mechanisms by which auxin controls these essential cellular responses are still poorly understood, despite recent progress in the identification of auxin receptors and components of auxin signaling pathways. The purpose of this review is to provide an overview of the present knowledge of the molecular mechanisms involved in the auxin control of cell division and cell expansion. In both cases, the involvement of at least two signaling pathways and of multiple targets of auxin action reflects the complexity of the subtle regulation of auxin-mediated cellular responses. In addition, it offers the necessary flexibility for generating differential responses within a given cell depending on its developmental context.

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“…This time lag could be attributed by an explanation that the auxin-binding site inhibited by PCIB may be located inside the cell and lag-period may be due to the time required for PCIB entering into the cells. Although there are some evidences that a functional extracellular auxinbinding protein perceives auxin signal (Steffens et al, 2001), the presence of auxin uptake carriers such as AUX1 and altered physiology of aux1 mutants indicate that auxin signal for root growth is perceived intracellularly. The fact that the lack of AUX1 affected the expression level of Aux/IAA genes and BA::GUS transgene (Abel et al, 1995;Oono et al, 1998) strongly suggests that expression level of auxin-regulated gene is also controlled by intracellular auxin.…”

Section: Pcib Disturbs Auxin Signaling At the Upstream Of Auxin-mediamentioning

confidence: 99%

p-Chlorophenoxyisobutyric Acid Impairs Auxin Response in Arabidopsis Root

et al. 2003

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p-Chlorophenoxyisobutyric acid (PCIB) is known as a putative antiauxin and is widely used to inhibit auxin action, although the mechanism of PCIB-mediated inhibition of auxin action is not characterized very well at the molecular level. In the present work, we showed that PCIB inhibited BA::␤-glucuronidase (GUS) expression induced by indole-3-acetic acid (IAA), 2,4-dichlorophenoxyacetic acid, and 1-naphthaleneacetic acid. PCIB also inhibited auxin-dependent DR5::GUS expression. RNA hybridization and quantitative reverse transcriptase-polymerase chain reaction analyses suggested that PCIB reduced auxin-induced accumulation of transcripts of Aux/IAA genes. In addition, PCIB relieved the reduction of GUS activity in HS::AXR3NT-GUS transgenic line in which auxin inhibits GUS activity by promoting degradation of the AXR3NT-GUS fusion protein. Physiological analysis revealed that PCIB inhibited lateral root production, gravitropic response of roots, and growth of primary roots. These results suggest that PCIB impairs auxin-signaling pathway by regulating Aux/IAA protein stability and thereby affects the auxin-regulated Arabidopsis root physiology.The plant hormone auxin (indole-3-acetic acid [IAA]) plays an important role in every aspect of plant growth and development (Thimann, 1977; Davies, 1995). Despite its physiological significance, the molecular mechanism of auxin action is not fully understood yet. One of the earliest events in the auxin action involves the changing of expression pattern of some specific genes with a lag period of 5 to 30 min (Abel and Theologis, 1996). Auxin-dependent degradation of Aux/IAA proteins is a key event for early auxin-dependent gene induction (Leyser, 2002). Aux/IAA proteins interact with auxin response factors (ARFs) that bind to auxin-responsive elements (AuxREs) in the auxin-responsive promoters (Guilfoyle, 1998). Aux/IAA proteins are short-lived proteins, and their stability is regulated by auxin through the ubiquitin-mediated protein degradation pathway (Leyser, 2002). In the absence of auxin, large amounts of Aux/IAA proteins are present, bind to ARFs, and prevent ARFs to activate transcription of auxin-induced genes from AuxREs. In the presence of auxin, degradation of Aux/IAA proteins is promoted, and then ARF proteins are released from Aux/IAA proteins and activate transcription of auxin-responsive genes (Tiwari et al., 2003). Although detailed molecular mechanism of the role of ARF and Aux/IAA proteins and their regulation has been revealed in these recent years, the mechanisms of the very early step of auxin signaling, i.e. how auxin is recognized by plant cell and how ubiquitin proteolysis system is activated, still remains unknown (Benfey, 2002).p-Chlorophenoxyisobutyric acid (PCIB), also called ␣-(4-chlorophenoxy) isobutyric acid, 2-(p-chlorophenoxy)-2-methylpropionic acid, or clofibric acid, has been most widely used to inhibit auxin action (e.g. Kim et al., 2000;Xie et al., 2000). Because of the structural similarity of PCIB with a synthetic auxin 4-chlorophenoxyac...

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The auxin signal for protoplast swelling is perceived by extracellular ABP1

Cited by 108 publications

References 26 publications

AUXIN BINDING PROTEIN1: The Outsider

AUXIN BINDING PROTEIN1: The Outsider

Cellular Responses to Auxin: Division versus Expansion

p-Chlorophenoxyisobutyric Acid Impairs Auxin Response in Arabidopsis Root

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