Regulation of Actin Filament Dynamics by Actin Depolymerizing Factor/Cofilin and Actin-Interacting Protein 1:  New Blades for Twisted Filaments

Ono, Shoichiro

doi:10.1021/bi034600x

Cited by 178 publications

(202 citation statements)

References 127 publications

(179 reference statements)

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“…The forms differ in their filament severing and depolymerizing abilities and tissue locations. UNC-60A is required for proper early development and UNC-60B for muscle sarcomere structure (Ono and Benian, 1998;Ono et al, 1999Ono et al, , 2003Ono, 2003;Yamashiro et al, 2005). The C-terminal portion of UNC-60B is critical for its interactions with filamentous actin .…”

Section: Thin Filamentmentioning

confidence: 99%

“…UNC-60B interacts with another actin severing protein, actin-interacting protein 1, coded for by the UNC-78 gene, that is also required for proper muscle thin filament assembly (Ono, 2001;Mohri and Ono, 2003;Mohri et al, 2006). This protein has two sevenblade propellers at each end of the protein that interact with the thin filament, and the UNC-60B actin depolymerizing factor/cofilin protein binds to the filament by wedging between the propellers (Ono, 2003;Mohri et al, 2004;Clark et al, 2006). Tropomyosin inhibits actin depolymerizing factor/cofilin activity (Ono and Ono, 2002;Yu and Ono, 2006).…”

Section: Thin Filamentmentioning

confidence: 99%

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Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

124

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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Section: Thin Filamentmentioning

confidence: 99%

Section: Thin Filamentmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

124

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“…AIP1, a conserved eukaryotic protein, enhances ADF/cofilin's actin filament disassembly activity (Ono, 2003). It is well established that AIP1 and ADF/cofilin interact in animals, plants, and fungi based on yeast two-hybrid screens (Rodal et al, 1999;Allwood et al, 2002), genetic interactions (Iida and Yahara, 1999;Rodal et al, 1999), and affinity chromatography (Okada et al, 1999), demonstrating the broad conservation of this interaction.…”

Section: Introductionmentioning

confidence: 99%

Actin Interacting Protein1 and Actin Depolymerizing Factor Drive Rapid Actin Dynamics inPhyscomitrella patens

et al. 2011

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The remodeling of actin networks is required for a variety of cellular processes in eukaryotes. In plants, several actin binding proteins have been implicated in remodeling cortical actin filaments (F-actin). However, the extent to which these proteins support F-actin dynamics in planta has not been tested. Using reverse genetics, complementation analyses, and cell biological approaches, we assessed the in vivo function of two actin turnover proteins: actin interacting protein1 (AIP1) and actin depolymerizing factor (ADF). We report that AIP1 is a single-copy gene in the moss Physcomitrella patens. AIP1 knockout plants are viable but have reduced expansion of tip-growing cells. AIP1 is diffusely cytosolic and functions in a common genetic pathway with ADF to promote tip growth. Specifically, ADF can partially compensate for loss of AIP1, and AIP1 requires ADF for function. Consistent with a role in actin remodeling, AIP1 knockout lines accumulate F-actin bundles, have fewer dynamic ends, and have reduced severing frequency. Importantly, we demonstrate that AIP1 promotes and ADF is essential for cortical F-actin dynamics.

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“…AIP1 is an actin regulatory protein found in a wide range of eukaryotic species which enhances ADF/cofilin-induced actin disassembly by capping ends of severed filaments, thus preventing elongation from the barbed ends [Ono, 2003]. Accordingly, the in vitro actin-depolymerizing activity of lily pollen LIADF1 is massively increased in the presence of AIP1 .…”

Section: Actin Bundling Versus Depolymerization Forcesmentioning

confidence: 99%

Actin bundling in plants

Thomas

Tholl

Moes

et al. 2009

Cell Motil. Cytoskeleton

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Tight regulation of plant actin cytoskeleton organization and dynamics is crucial for numerous cellular processes including cell division, expansion and intracellular trafficking. Among the various actin regulatory proteins, actin-bundling proteins trigger the formation of bundles composed of several parallel actin filaments closely packed together. Actin bundles are present in virtually all plant cells, but their biological roles have rarely been addressed directly. However, decades of research in the plant cytoskeleton field yielded a bulk of data from which an overall picture of the functions supplied by actin bundles in plant cells emerges. Although plants lack several equivalents of animal actin-bundling proteins, they do possess major bundler classes including fimbrins, villins and formins. The existence of additional players is not excluded as exemplified by the recent characterization of plant LIM proteins, which trigger the formation of actin bundles both in vitro and in vivo. This apparent functional redundancy likely reflects the need for plant cells to engineer different types of bundles that act at different sub-cellular locations and exhibit specific function-related properties. By surveying information regarding the properties of plant actin bundles and their associated bundling proteins, the present review aims at clarifying why and how plants make actin bundles. Cell Motil. Cytoskeleton 66: 940-957, 2009. '

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Regulation of Actin Filament Dynamics by Actin Depolymerizing Factor/Cofilin and Actin-Interacting Protein 1: New Blades for Twisted Filaments

Cited by 178 publications

References 127 publications

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Actin Interacting Protein1 and Actin Depolymerizing Factor Drive Rapid Actin Dynamics inPhyscomitrella patens

Actin bundling in plants

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