Identification and Characterization of a Novel Microtubule-Based Motor Associated with Membranous Organelles in Tobacco Pollen Tubes

Cai, Giampiero; Romagnoli, Silvia; Moscatelli, Alessandra; Ovidi, Elisa; Gambellini, Gabriella; Tiezzi, Antonio; Cresti, Mauro

doi:10.1105/tpc.12.9.1719

Cited by 61 publications

(29 citation statements)

References 62 publications

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“…Except for a role in cell plate formation and pollen tube organelle movements (17,88,89), there is little experimental evidence for involvement of microtubules in the trafficking of subcellular components in higher plants (36,56). Thus, it was surprising that the MP-GFP so obviously decorated the cortical microtubule network (41,42).…”

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confidence: 99%

Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

Ashby

Boutant

Seemanpillai

et al. 2006

J Virol

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The cell-to-cell spread of Tobacco mosaic virus infection depends on virus-encoded movement protein (MP), which is believed to form a ribonucleoprotein complex with viral RNA (vRNA) and to participate in the intercellular spread of infectious particles through plasmodesmata. Previous studies in our laboratory have provided evidence that the vRNA movement process is correlated with the ability of the MP to interact with microtubules, although the exact role of this interaction during infection is not known. Here, we have used a variety of in vivo and in vitro assays to determine that the MP functions as a genuine microtubule-associated protein that binds microtubules directly and modulates microtubule stability. We demonstrate that, unlike MP in whole-cell extract, microtubule-associated MP is not ubiquitinated, which strongly argues against the hypothesis that microtubules target the MP for degradation. In addition, we found that MP interferes with kinesin motor activity in vitro, suggesting that microtubule-associated MP may interfere with kinesin-driven transport processes during infection.

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confidence: 99%

Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

Ashby

Boutant

Seemanpillai

et al. 2006

J Virol

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“…2 and 5), although the role of MTs in pollen development remains elusive. Recent characterization of pollen-specific kinesinrelated motor proteins (Cai et al, 2000;Romagnoli et al, 2003) and MT-associated protein (Huang et al, 2007) support MT's participation with actin filaments in directing vesicle and organelle transport in elongating pollen tubes. MTs likely play a role in deposition of pollen cell wall components, e.g.…”

Section: Discussionmentioning

confidence: 99%

Differential Expansion and Expression ofα- andβ-Tubulin Gene Families inPopulus

et al. 2007

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Microtubule organization is intimately associated with cellulose microfibril deposition, central to plant secondary cell wall development. We have determined that a relatively large suite of eight a-TUBULIN (TUA) and 20 b-TUBULIN (TUB) genes is expressed in the woody perennial Populus. A number of features, including gene number, a:b gene representation, amino acid changes at the C terminus, and transcript abundance in wood-forming tissue, distinguish the Populus tubulin suite from that of Arabidopsis thaliana. Five of the eight Populus TUAs are unusual in that they contain a C-terminal methionine, glutamic acid, or glutamine, instead of the more typical, and potentially regulatory, C-terminal tyrosine. Both C-terminal Y-type (TUA1) and M-type (TUA5) TUAs were highly expressed in wood-forming tissues and pollen, while the Y-type TUA6 and TUA8 were abundant only in pollen. Transcripts of the disproportionately expanded TUB family were present at comparatively low levels, with phylogenetically distinct classes predominating in xylem and pollen. When tension wood induction was used as a model system to examine changes in tubulin gene expression under conditions of augmented cellulose deposition, xylem-abundant TUA and TUB genes were up-regulated. Immunolocalization of TUA and TUB in xylem and phloem fibers of stems further supported the notion of heavy microtubule involvement during cellulose microfibril deposition in secondary walls. The high degree of sequence diversity, differential expansion, and differential regulation of Populus TUA and TUB families may confer flexibility in cell wall formation that is of adaptive significance to the woody perennial growth habit.

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“…Samples were observed at the optical microscope under DIC view. Motility of microtubules was recorded according to the literature [28].…”

Section: In Vitro Motility Assaysmentioning

confidence: 99%

Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments

Duca

Serafini-Fracassini

Bonner

et al. 2009

Biochemical Journal

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TGases (transglutaminases) are a class of calcium-dependent enzymes that catalyse the interactions between acyl acceptor glutamyl residues and amine donors, potentially making crosslinks between proteins. To assess the activity of apple (Malus domestica) pollen TGase on the functional properties of actin and tubulin, TGase was prepared from apple pollen by hydrophobic interaction chromatography and assayed on actin and tubulin purified from the same cell type. The enzyme catalysed the incorporation of putrescine in the cytoskeleton monomers. When tested on actin filaments, pollen TGase induced the formation of high-molecular-mass aggregates of actin. Use of fluoresceincadaverine showed that the labelled polyamine was incorporated into actin by pollen TGase, similar to with guinea pig liver TGase. The pollen TGase also reduced the enzyme activity and the binding of myosin to TGase-treated actin filaments. Polymerization of tubulin in the presence of pollen TGase also yielded the formation of high molecular mass aggregates. Furthermore, the pollen TGase also affected the binding of kinesin to microtubules and reduced the motility of microtubules along kinesincoated slides. These results indicate that the pollen TGase can control different properties of the pollen tube cytoskeleton (including the ability of actin and tubulin to assemble and their interaction with motor proteins) and consequently regulate the development of pollen tubes.

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Identification and Characterization of a Novel Microtubule-Based Motor Associated with Membranous Organelles in Tobacco Pollen Tubes

Cited by 61 publications

References 62 publications

Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

Differential Expansion and Expression ofα- andβ-Tubulin Gene Families inPopulus

Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments

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