Novel components of the plant cytoskeleton: a beginning to plant ‘cytomics’

Davies, Eric; Stanković, Bratislav; Azama, Kishu; Shibata, Koichi; Abe, Shunnosuke

doi:10.1016/s0168-9452(00)00365-4

Cited by 29 publications

(18 citation statements)

References 66 publications

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“…1C) and LC-MS/MS (Table III), EF-1␣ (spot 38) was an abundant protein in the tubulin-binding protein fraction. Several other elongation and initiation factors were also identified, some of which have been shown to bind to MTs and other cytoskeletal structures in previous studies (Table III) (12,(43)(44)(45)(46). These included EF-2 (spot 4) and subunits of the eukaryotic translation initiation factors eIF3 and eIF4 (spots 7,18,24,27,50,54,70).…”

Section: Resultsmentioning

confidence: 77%

“…Using a detergent-resistant cytoskeleton/ protein body fraction from rice and maize endosperm cells, 15 and 5 cytoskeleton-associated proteins were identified, respectively (21,22). Another plant study identified 8 proteins from a detergent-resistant protein fraction from pea stems (12). Here we report the identification of 122 proteins that were purified from an Arabidopsis cell suspension culture extract using tubulin affinity chromatography.…”

mentioning

confidence: 93%

“…The addition of high concentrations of neuronal MTs has been used as an alternative to facilitate the recovery of MT-binding proteins (7). Modifications to these techniques have been aimed at eliminating problems associated with the tough cell wall and lytic vacuoles in plant cells, and the development of "gentle" extraction buffers that maintain cytoskeleton integrity has made the plant cytoskeleton purification procedure more efficient (12).…”

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confidence: 99%

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Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Chuong

Good

Taylor

et al. 2004

Molecular & Cellular Proteomics

112

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Microtubules play an essential role in the growth and development of plants and are known to be involved in regulating many cellular processes ranging from translation to signaling. In this article, we describe the proteomic characterization of Arabidopsis tubulin-binding proteins that were purified using tubulin affinity chromatography. Microtubule co-sedimentation assays indicated that most, if not all, of the proteins in the tubulin-binding protein fraction possessed microtubule-binding activity. Two-dimensional gel electrophoresis of the tubulin-binding protein fraction was performed, and 86 protein spots were excised and analyzed for protein identification. A total of 122 proteins were identified with high confidence using LC-MS/MS. These proteins were grouped into six categories based on their predicted functions: microtubule-associated proteins, translation factors, RNA-binding proteins, signaling proteins, metabolic enzymes, and proteins with other functions. Almost one-half of the proteins identified in this fraction were related to proteins that have previously been reported to interact with microtubules. This study represents the first large-scale proteomic identification of eukaryotic cytoskeleton-binding proteins, and provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells. Molecular & Cellular Proteomics 3:970 -983, 2004.The cytoskeleton is the single most important structure that contributes to the highly ordered organization of the eukaryotic cell. It provides a framework for cell division and the trafficking of organelles and macromolecules, and also serves to regulate important cellular processes such as signaling, translation, and metabolism. The cytoskeleton plays a key role in a number of plant-specific processes, such as assisting in the formation of the cell plate, regulating cell-to-cell movement, and influencing the direction of cell elongation (1). A role for the microtubule (MT) 1 component of the cytoskeleton in many of these processes has been demonstrated, and a number of MT-binding proteins that are responsible for regulating these events have been identified.Plant MTs are assembled into four distinct arrays during the cell cycle (2). Three of these arrays-the interphase cortical array, the pre-prophase band, and the phragmoplast-have no counterpart in animal cells. The cortical MT array has been linked to the regulation of cellulose microfibril deposition and, hence, a role in cell expansion, while the pre-prophase band and the phragmoplast have important roles in the positioning and synthesis of the new cell plate in dividing cells. The fourth array, the spindle, has an evolutionarily conserved role in the segregation of chromosomes during cell division. The organization and dynamics of MTs in these arrays depend on the activity of various MT-associated proteins (MAPs). Several plant MAPs have been identified, including the 65-kDa MAPs, MAP 190, and MOR1 (3). These proteins are important in cross-bridging MTs, linking MTs with actin filamen...

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Section: Resultsmentioning

confidence: 77%

mentioning

confidence: 93%

mentioning

confidence: 99%

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Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Chuong

Good

Taylor

et al. 2004

Molecular & Cellular Proteomics

112

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“…For example, apyrase can locate to the nucleus and the cytoskeleton where it is likely to be involved in mRNA transport, and also in the extracellular matrix where it functions in the phosphate transport and xenobiotic resistance [52]. In addition, citrate synthase has a mitochondrial targeting sequence, yet it can also exist in the cytoplasm where it forms filaments that bind the eukaryotic elongation factor eEF1a [53].…”

Section: Contamination or Alternative Secretory Pathway?mentioning

confidence: 99%

“…In addition, citrate synthase has a mitochondrial targeting sequence, yet it can also exist in the cytoplasm where it forms filaments that bind the eukaryotic elongation factor eEF1a [53]. Davies et al [52] conceded that despite the possibility of predicting subcellular location of a protein from its amino acid sequence, slight post-translational modifications may allow multiple locations and/or functions for the same protein. Therefore, the proteins without a predicted signal sequence that were identified in this study and are also known to be secreted in other species, appear to be exported to the cell wall via an unknown mechanism.…”

Section: Contamination or Alternative Secretory Pathway?mentioning

confidence: 99%

Proteomic analysis of the Arabidopsis thaliana cell wall

et al. 2002

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With the completion of the Arabidopsis genome, many hypothetical proteins have been predicted without any information on their expression, subcellular localisation and function. We have performed proteomic analysis of proteins sequentially extracted from enriched Arabidopsis cell wall fractions and separated by two-dimensional gel electrophoresis (2-DE). The proteins were identified by peptide mass fingerprinting using matrix-assisted laser desorption/ionisation-time of flight (MALDI-TOF) mass spectrometry and genomic database searches. This is part of a targeted exercise to establish the entire Arabidopsis secretome database. We report evidence for new proteins of unknown function whose existence had been predicted from genomic sequences and, furthermore, localise them to the cell wall. In addition, we observed an unexpected presence in the cell wall preparations of proteins whose known biochemical activity has never been associated with this compartment hitherto. We discuss the implications of these findings and present results suggesting a possible involvement of cell wall kinases in plant responses to pathogen attack.

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Plant Proteomics

Saravanan¹,

Bashir²,

Rose³

2004

Handbook of Plant Biotechnology

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Proteomics, or the study of the protein complement of the genome, promises to help bridge the divide between genomic DNA sequence and biological state and represents one of the most rapidly developing and innovative fields in genome‐scale research. The term is now commonly and broadly used to encompass almost any aspect of protein structure, expression and function. However, as used here it refers to characterising quantitative and qualitative characteristics of global protein expression, with an emphasis on scale, including polypeptide synthesis, degradation, post‐translational modification, the structure of protein complexes and interactions with other proteins and cellular components. The systematic characterisation of complex protein populations can be pursued using many approaches and numerous reviews have recently been published describing developments in diverse areas of proteomics, including protein structure, function and protein–protein, or protein–ligand interactions A number of reviews have also been specifically devoted to plant proteomics. Consequently, the multiplicity of proteomics‐related experimentation and developing technologies are not reiterated here in detail. Instead, this chapter intends to provide an overview of the diversity of proteomics‐based studies that have been reported in plants to date and emerging technologies, which in turn should underscore the tremendous potential utility of proteomics for plant biologists and give an indication of future applications.

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Novel components of the plant cytoskeleton: a beginning to plant ‘cytomics’

Cited by 29 publications

References 66 publications

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Proteomic analysis of the Arabidopsis thaliana cell wall

Plant Proteomics

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