Profilin as a regulator of the membrane-actin cytoskeleton interface in plant cells

Sun, Tao; Li, Shanwei; Ren, Haiyun

doi:10.3389/fpls.2013.00512

Cited by 52 publications

(35 citation statements)

References 83 publications

(90 reference statements)

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“…The higher order organization of the actin cytoskeleton consists mostly of bundles and cables, and their assembly into these structures is specified by several actin binding proteins such as fimbrin, villin, profilin, LIM domain-containing proteins, thrumin, and crolin (Papuga et al, 2010;Whippo et al, 2011;Su et al, 2012;Jia et al, 2013;Qu et al, 2013;Sun et al, 2013). The movement and dynamics of the ER and the various organelles that make up the plant endomembrane system are largely dependent on the actin cytoskeleton, as demonstrated using actin-disrupting drugs such as latrunculin B (LatB) and cytochalasin D (Boevink et al, 1998;Nebenführ et al, 1999;Sparkes et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Many of these proteins, such as the ARP2/3 complex, profilin, formins, and capping proteins, which localize to the PM and various membranes of organelles within the endomembrane system, have orthologs in other eukaryotes (Zhang et al, 2010Sun et al, 2013;Jimenez-Lopez et al, 2014;Cvr cková et al, 2015). In fact, some of the mechanisms by which F-actin on membranes is nucleated and polymerized in plants mirror those of animals and yeast, where small GTPases of the Rho family directly activate membrane-localized actin nucleators (Takenawa and Suetsugu, 2007).…”

Section: Introductionmentioning

confidence: 99%

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HLB1 Is a Tetratricopeptide Repeat Domain-Containing Protein That Operates at the Intersection of the Exocytic and Endocytic Pathways at the TGN/EE in Arabidopsis

et al. 2016

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The endomembrane system plays essential roles in plant development, but the proteome responsible for its function and organization remains largely uncharacterized in plants. Here, we identified and characterized the HYPERSENSITIVE TO LATRUNCULIN B1 (HLB1) protein isolated through a forward-genetic screen in Arabidopsis thaliana for mutants with heightened sensitivity to actin-disrupting drugs. HLB1 is a plant-specific tetratricopeptide repeat domain-containing protein of unknown function encoded by a single Arabidopsis gene. HLB1 associated with the trans-Golgi network (TGN)/early endosome (EE) and tracked along filamentous actin, indicating that it could link post-Golgi traffic with the actin cytoskeleton in plants. HLB1 was found to interact with the ADP-ribosylation-factor guanine nucleotide exchange factor, MIN7/BEN1 (HOPM INTERACTOR7/BREFELDIN A-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE1) by coimmunoprecipitation. The min7/ben1 mutant phenocopied the mild root developmental defects and latrunculin B hypersensitivity of hlb1, and analyses of a hlb1/ min7/ben1 double mutant showed that hlb1 and min7/ben1 operate in common genetic pathways. Based on these data, we propose that HLB1 together with MIN7/BEN1 form a complex with actin to modulate the function of the TGN/EE at the intersection of the exocytic and endocytic pathways in plants.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

HLB1 Is a Tetratricopeptide Repeat Domain-Containing Protein That Operates at the Intersection of the Exocytic and Endocytic Pathways at the TGN/EE in Arabidopsis

et al. 2016

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“…Por lo que al haber sido ofrecido el alimento en forma de harina, la proteína pudo haberse estratificado y el animal haber consumido una mayor proporción de fracciones grandes, las cuales tienen una mayor proporción de proteína ligada a la fibra como la proteína extensina (39)(40)(41) ; una menor digestibilidad de la proteína en las fracciones pequeñas en relación a las fracciones grandes también fue observada en la pasta de soya (42) . La digestibilidad de la proteína de los subproductos de cártamo (SPC y pasta) fue similar a la reportada para la pastas de canola y girasol (21,43,44) , y granos secos de destilería (45) ; aunque la digestibilidad de la energía y el contenido de energía digestible de los subproductos de cártamo (SPC y Pasta) fue menor a la reportada para esas materias primas (21,43,45) .…”

Section: Discussionunclassified

Valor nutritivo de subproductos de cártamo para cerdos en finalización

Landín

Rodríguez

Ibargüengoytia³

2017

Rev. Mex. Cienc. Pecu.

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RESUMENPara determinar en subproductos de cártamo la digestibilidad aparente del tracto total (DATT) de materia seca (MS), proteína cruda (PC) y energía (En); y las digestibilidades aparente ileal (DAI) y estandarizada ileal (DEI) de aminoácidos (AA), se realizaron dos experimentos. En el primero se utilizaron cinco cerdos de 50 ± 3.5 kg bajo un diseño en cuadro latino 5 x 5. Se evaluaron dos subproductos de cártamo (SPC, pasta), en dos presentaciones: molida y sin moler. Se formuló una dieta testigo de caseína y cuatro experimentales de subproductos de cártamo y caseína. En el segundo se utilizaron ocho cerdos de 35.0 ± 2.5 kg canulados a nivel ileal. Se emplearon los subproductos molidos para fabricar tres dietas: una testigo de caseína y dos experimentales de subproductos de cártamo (pasta y SPC) y caseína. En el primer periodo los animales consumieron las dietas experimentales (cuatro cerdos por tratamiento); en el segundo todos consumieron la dieta testigo. Los resultados mostraron que fue mayor la DATT (P <0.05) de PC de la pasta (87.4 en promedio); intermedia en el SPC sin moler (83.7) e inferior en el SPC molido (76.0). La DATT de En fue mayor (P <0.05) en los SPC (64.5 en promedio) que en la Pasta (57.5 en promedio). La DAI y DEI de PC y AA de ambos subproductos fue similar (P >0.05) entre ellos. Se concluye que el contenido de energía digestible de los subproductos de cártamo es bajo (1,419 a 1,738 kcal/kg) y la DEI de los AA fue similar entre ellos.PALABRAS CLAVE: Cártamo, Energía, Aminoácidos, Digestibilidad, Cerdos. ABSTRACT To determine the apparent total tract digestibility (ATTD) of dry matter (DM), crude protein (CP) and energy (E).And the apparent and standardized ileal digestibility (AID, SID) of amino acids (AA) in safflower coproducts, two experiments were conducted. In the first five pigs of 50 ± 3.5 kg under a latin square design 5 x 5 two safflower coproducts (byproduct, meal) were evaluated using two presentations each: Ground and unground. Five diets were formulated: control (casein) and four experimental (safflower coproducts and casein). In the second experiment, eight pigs of 35.0 ± 2.5 kg cannulated at the ileal level were used. The ground meals were used to fabricate three diets: a reference (casein) and two experimental (safflower coproducts and casein). In the first experimental period, the pigs consumed the experimental diets (four pigs per treatment); in the second period, all pigs consumed the reference diet. The digestibility was analyzed according to a completely randomized design. The ATTD of CP was higher (P <0.05) on meal (87.4 in average); intermediate in by product unground (83.7) and lower in by product ground (76.0). The ATTD was higher (P <0.05) in by product (64.5 in average) than from Meal (57.7 in average). The AID and SID of CP and AA were similar (P >0.05) among coproducts. It is concluded that the SM digestible energy content is low (1.419 to 1.738 kcal/kg) and the SID of AA was similar among safflower coproducts.

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“…Sun et al (2013) briefly review the long history of discovery research surrounding this abundant regulator of actin dynamcis. Biochemically, isoforms from maize and Arabidopsis have been well characterized and these bind three cellular ligands: monomer of G-actin, proteins with contiguous stretches of proline residues, and phosphoinositide lipids.…”

Section: Actin-binding Proteins: Old and Newmentioning

confidence: 99%

A dynamic interplay between membranes and the cytoskeleton critical for cell development and signaling

2014

Frontiers Research Topics

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Diverse cellular processes that underlie plant development and response to environmental cues rely on a dynamic interplay between membranes and the cytoskeleton. The original research and review articles assembled in this Research Topic provide a valuable insight into our current understanding of how actin filaments and microtubules physically and functionally interact with membranes and cell wall and vice versa. ACTIN-BINDING PROTEINS: OLD AND NEWActin-binding proteins come in hundreds of different varieties and are the governors for cellular cytoskeletal organization and turnover. The rate limiting step for generating actin filaments from a monomer pool in vitro, and presumably in vivo, is formation of a seed or nucleus of three actin subunits. Formins are conserved actin nucleation factors which, in plants, take on special relevance for the presence of secretion signals, transmembrane domains and lipid interaction motifs that permit their function on or near cellular membranes. In an up-to-date review, Cvrčková (2013) discusses the myriad ways that plant formins are thought to associate with membranes and their function(s) at various subcellular locations, especially the interface between cortical actin cytoskeleton-plasma membrane-cell wall.The monomer-binding protein, profilin, was the first conventional plant actin-binding protein to be identified more than two decades ago. Sun et al. (2013) briefly review the long history of discovery research surrounding this abundant regulator of actin dynamcis. Biochemically, isoforms from maize and Arabidopsis have been well characterized and these bind three cellular ligands: monomer of G-actin, proteins with contiguous stretches of proline residues, and phosphoinositide lipids. More recently, it has been discovered that plant profilins are localized or function at cellular membranes and organelles via their interaction with nucleators like the formins; here, profilinactin complexes likely provide a supply of subunits to polymerize new actin filaments. Whether this actin assembly powers vesicle or organelle movements, as in the case of mammalian endosomes or pathogenic intracellular bacteria, is an area for future investigations.One striking difference between the repertoire of actinbinding proteins from plants and animals is that many types of actin-membrane adaptors present in animals are absent from plants. Plants in turn own a plant-specific superfamily of actin-binding proteins, called the Networked (NET) proteins; presumably these are able to connect actin filaments to various membrane compartments. Here, Hawkins et al. (2014) report a phylogenetic analysis including NET gene sequences across a large range of species. Their data support that the NET superfamily emerged early in the evolution of vascular plants and has continuously developed and diversified coincidentally with the complexity of plant species. CORTICAL MICROTUBULES AND CELL WALL ASSEMBLYA remarkable parallelism between membrane-associated microtubules in the cortical cytoplasm and cellulose micro...

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Profilin as a regulator of the membrane-actin cytoskeleton interface in plant cells

Cited by 52 publications

References 83 publications

HLB1 Is a Tetratricopeptide Repeat Domain-Containing Protein That Operates at the Intersection of the Exocytic and Endocytic Pathways at the TGN/EE in Arabidopsis

HLB1 Is a Tetratricopeptide Repeat Domain-Containing Protein That Operates at the Intersection of the Exocytic and Endocytic Pathways at the TGN/EE in Arabidopsis

Valor nutritivo de subproductos de cártamo para cerdos en finalización

A dynamic interplay between membranes and the cytoskeleton critical for cell development and signaling

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