Hsp90 binds microtubules and is involved in the reorganization of the microtubular network in angiosperms

Krtková, Jana; Zimmermann, Aleksandra; Schwarzerová, Kateřina; Nick, Peter

doi:10.1016/j.jplph.2012.06.010

Cited by 14 publications

(15 citation statements)

References 75 publications

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“…Other proteins generally recovered in microtubule pull-down experiments, and which decorate microtubule structures (e.g., the spindle), were also found, such as GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (Kumagai and Sakai, 1983), heat shock protein 70 (Parrotta et al, 2013), heat shock protein 90 (Petrášek et al, 1998;Krtková et al, 2012), clathrin heavy chains (Royle, 2012), and elongation factor 1a (Hugdahl et al, 1995). Comparison with other Arabidopsis proteomic data sets focusing on identification of proteins binding to tubulin or microtubules (Chuong et al, 2004;Korolev et al, 2005;Hamada et al, 2013) revealed 64 proteins common to our data set (Supplemental Data Set 3).…”

Section: Proteomic Analysis Of Microtubule Interacting Proteins Durinmentioning

confidence: 90%

Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis

et al. 2015

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Plant vascular cells, or tracheary elements (TEs), rely on circumferential secondary cell wall thickenings to maintain sap flow. The patterns in which TE thickenings are organized vary according to the underlying microtubule bundles that guide wall deposition. To identify microtubule interacting proteins present at defined stages of TE differentiation, we exploited the synchronous differentiation of TEs in Arabidopsis thaliana suspension cultures. Quantitative proteomic analysis of microtubule pull-downs, using ratiometric 14 N/ 15 N labeling, revealed 605 proteins exhibiting differential accumulation during TE differentiation. Microtubule interacting proteins associated with membrane trafficking, protein synthesis, DNA/ RNA binding, and signal transduction peaked during secondary cell wall formation, while proteins associated with stress peaked when approaching TE cell death. In particular, CELLULOSE SYNTHASE-INTERACTING PROTEIN1, already associated with primary wall synthesis, was enriched during secondary cell wall formation. RNAi knockdown of genes encoding several of the identified proteins showed that secondary wall formation depends on the coordinated presence of microtubule interacting proteins with nonoverlapping functions: cell wall thickness, cell wall homogeneity, and the pattern and cortical location of the wall are dependent on different proteins. Altogether, proteins linking microtubules to a range of metabolic compartments vary specifically during TE differentiation and regulate different aspects of wall patterning.

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Section: Proteomic Analysis Of Microtubule Interacting Proteins Durinmentioning

confidence: 90%

Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis

et al. 2015

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“…Additionally, microtubules are involved in P-body dynamics (Sweet et al, 2007;Aizer et al, 2008). A limited association between microtubules and the ER, P-bodies (Hamada et al, 2012), and HSP90 has also been reported in plants (Krtková et al, 2012). Alteration of the microtubule network may affect the trafficking or assembly of cellular compartments required for translational inhibition.…”

Section: Cytoskeletonmentioning

confidence: 99%

Biogenesis, Turnover, and Mode of Action of Plant MicroRNAs

2013

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(K.R.).MicroRNAs (miRNAs) are small RNAs that control gene expression through silencing of target mRNAs. Mature miRNAs are processed from primary miRNA transcripts by the endonuclease activity of the DICER-LIKE1 (DCL1) protein complex. Mechanisms exist that allow the DCL1 complex to precisely excise the miRNA from its precursor. Our understanding of miRNA biogenesis, particularly its intersection with transcription and other aspects of RNA metabolism such as splicing, is still evolving. Mature miRNAs are incorporated into an ARGONAUTE (AGO) effector complex competent for target gene silencing but are also subjected to turnover through a degradation mechanism that is beginning to be understood. The mechanisms of miRNA target silencing in plants are no longer limited to AGO-catalyzed slicing, and the contribution of translational inhibition is increasingly appreciated. Here, we review the mechanisms underlying the biogenesis, turnover, and activities of plant miRNAs.

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“…The kinetics of tubulin acetylation correlated well with the kinetics of Hsp90 upregulation, suggesting that Hsp90 might be involved in acetylation of α-tubulin. In addition, previous studies have demonstrated that Hsp90 binds MTs and is involved in the reorganization of the microtubular network [24]. Thus we tested the correlation between Hsp90 and tubulin (Fig.…”

Section: Resultsmentioning

confidence: 99%

Heat-Shock Protein 90 Promotes Nuclear Transport of Herpes Simplex Virus 1 Capsid Protein by Interacting with Acetylated Tubulin

et al. 2014

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Although it is known that inhibitors of heat shock protein 90 (Hsp90) can inhibit herpes simplex virus type 1 (HSV-1) infection, the role of Hsp90 in HSV-1 entry and the antiviral mechanisms of Hsp90 inhibitors remain unclear. In this study, we found that Hsp90 inhibitors have potent antiviral activity against standard or drug-resistant HSV-1 strains and viral gene and protein synthesis are inhibited in an early phase. More detailed studies demonstrated that Hsp90 is upregulated by virus entry and it interacts with virus. Hsp90 knockdown by siRNA or treatment with Hsp90 inhibitors significantly inhibited the nuclear transport of viral capsid protein (ICP5) at the early stage of HSV-1 infection. In contrast, overexpression of Hsp90 restored the nuclear transport that was prevented by the Hsp90 inhibitors, suggesting that Hsp90 is required for nuclear transport of viral capsid protein. Furthermore, HSV-1 infection enhanced acetylation of α-tubulin and Hsp90 interacted with the acetylated α-tubulin, which is suppressed by Hsp90 inhibition. These results demonstrate that Hsp90, by interacting with acetylated α-tubulin, plays a crucial role in viral capsid protein nuclear transport and may provide novel insight into the role of Hsp90 in HSV-1 infection and offer a promising strategy to overcome drug-resistance.

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Hsp90 binds microtubules and is involved in the reorganization of the microtubular network in angiosperms

Cited by 14 publications

References 75 publications

Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis

Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis

Biogenesis, Turnover, and Mode of Action of Plant MicroRNAs

Heat-Shock Protein 90 Promotes Nuclear Transport of Herpes Simplex Virus 1 Capsid Protein by Interacting with Acetylated Tubulin

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