Cooperation of two actin‐binding proteins, cofilin and Aip1, in <i>Saccharomyces cerevisiae</i>

Iida, Kei; Yahara, Ichiro

doi:10.1046/j.1365-2443.1999.00235.x

Cited by 64 publications

(71 citation statements)

References 43 publications

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“…However, synthetic lethal interactions occur when an AIP1 deletion is combined with specific cofilin alleles (Iida and Yahara, 1999;Rodal et al, 1999), confirming a biological role for Aip1p in yeast. Furthermore, partial mislocalization of cofilin from cortical patches to actin cables has been observed in an aip1⌬ yeast strain (Rodal et al, 1999).…”

Section: Introductionmentioning

confidence: 87%

“…Subsequent twohybrid analysis identified a physical interaction between Aip1p and cofilin (Rodal et al, 1999), although biochemical and two-hybrid analyses suggested that the interaction is stabilized by actin (Rodal et al, 1999). Aip1p was also found to be functionally related to cofilin because of its ability to suppress a cof1 temperature-sensitive mutant upon overexpression (Iida and Yahara, 1999). Aip1p increases filament disassembly at low stoichiometry, but this is dependent upon cofilin decoration of the filament and is optimal when the ratio of cofilin to actin is 1:1 (Rodal et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

Clark

Teply

Haarer

et al. 2006

MBoC

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Actin interacting protein 1 (Aip1p) and cofilin cooperate to disassemble actin filaments in vitro and are thought to promote rapid turnover of actin networks in vivo. The precise method by which Aip1p participates in these activities has not been defined, although severing and barbed-end capping of actin filaments have been proposed. To better describe the mechanisms and biological consequences of Aip1p activities, we undertook an extensive mutagenesis of AIP1 aimed at disrupting and mapping Aip1p interactions. Site-directed mutagenesis suggested that Aip1p has two actin binding sites, the primary actin binding site lies on the edge of its N-terminal ␤-propeller and a secondary actin binding site lies in a comparable location on its C-terminal ␤-propeller. Random mutagenesis followed by screening for separation of function mutants led to the identification of several mutants specifically defective for interacting with cofilin but still able to interact with actin. These mutants suggested that cofilin binds across the cleft between the two propeller domains, leaving the actin binding sites exposed and flanking the cofilin binding site. Biochemical, genetic, and cell biological analyses confirmed that the actin binding-and cofilin binding-specific mutants are functionally defective, whereas the genetic analyses further suggested a role for Aip1p in an early, internalization step of endocytosis. A complementary, unbiased molecular modeling approach was used to derive putative structures for the Aip1p-cofilin complex, the most stable of which is completely consistent with the mutagenesis data. We theorize that Aip1p-severing activity may involve simultaneous binding to two actin subunits with cofilin wedged between the two actin binding sites of the N-and C-terminal propeller domains.

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Section: Introductionmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

Clark

Teply

Haarer

et al. 2006

MBoC

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“…AIP1 nulls are synthetic lethal with viable cofilin mutant alleles placing them in a common genetic pathway (Iida and Yahara, 1999;Rodal et al, 1999). Furthermore, AIP1 nulls aberrantly accumulate cofilin along actin cables (Iida and Yahara, 1999;Rodal et al, 1999), and these cables are less sensitive to turnover by latrunculin A (Okada et al, 2006). Collectively, these studies highlight a functional link between AIP1 and actin, demonstrating that AIP1 has evolved variable roles and requirements in fungi, animals, and slime molds.…”

Section: Introductionmentioning

confidence: 94%

“…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. AIP1 has negligible effects on actin filaments.…”

Section: Introductionmentioning

confidence: 99%

“…While AIP1 deletion in budding yeast does not result in any growth defects (Rodal et al, 1999), AIP1 is clearly involved in actin turnover. AIP1 nulls are synthetic lethal with viable cofilin mutant alleles placing them in a common genetic pathway (Iida and Yahara, 1999;Rodal et al, 1999). Furthermore, AIP1 nulls aberrantly accumulate cofilin along actin cables (Iida and Yahara, 1999;Rodal et al, 1999), and these cables are less sensitive to turnover by latrunculin A (Okada et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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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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Intracellular pH modulation of ADF/cofilin proteins

Bernstein

Painter

Chen

et al. 2000

Cell Motil. Cytoskeleton

123

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Cooperation of two actin‐binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae

Cited by 64 publications

References 43 publications

A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

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

Intracellular pH modulation of ADF/cofilin proteins

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