Dynamic Bridges—A Calponin-Domain Kinesin From Rice Links Actin Filaments and Microtubules in Both Cycling and Non-Cycling Cells

Frey, Nicole; Klotz, Jan; Nick, Peter

doi:10.1093/pcp/pcp094

Cited by 53 publications

(62 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Intriguingly, AFH14 decorates almost all mitotic and cytokinetic cytoskeletal apparatuses but does not localize to cortical cytoskeletal networks in interphase cells, which is different from the localization of PTEN-containing formins in moss (Vidali et al, 2009). In combination with our genetic, cellular, and biochemical studies, these results strongly suggest that AFH14 may have a function distinct from cytoskeletal linkers involved in interactions between microtubules and microfilaments in the cell cortex (Collings et al, 1998;Schwab et al, 2003;Preuss et al, 2004;Frey et al, 2009). …”

Section: Immunostaining Was Used To Assess Tubulin Localization In Wisupporting

confidence: 64%

The Type IIArabidopsisFormin14 Interacts with Microtubules and Microfilaments to Regulate Cell Division

et al. 2010

View full text Add to dashboard Cite

Formins have long been known to regulate microfilaments but have also recently been shown to associate with microtubules. In this study, Arabidopsis thaliana FORMIN14 (AFH14), a type II formin, was found to regulate both microtubule and microfilament arrays. AFH14 expressed in BY-2 cells was shown to decorate preprophase bands, spindles, and phragmoplasts and to induce coalignment of microtubules with microfilaments. These effects perturbed the process of cell division. Localization of AFH14 to microtubule-based structures was confirmed in Arabidopsis suspension cells. Knockdown of AFH14 in mitotic cells altered interactions between microtubules and microfilaments, resulting in the formation of an abnormal mitotic apparatus. In Arabidopsis afh14 T-DNA insertion mutants, microtubule arrays displayed abnormalities during the meiosis-associated process of microspore formation, which corresponded to altered phenotypes during tetrad formation. In vitro biochemical experiments showed that AFH14 bound directly to either microtubules or microfilaments and that the FH2 domain was essential for cytoskeleton binding and bundling. However, in the presence of both microtubules and microfilaments, AFH14 promoted interactions between microtubules and microfilaments. These results demonstrate that AFH14 is a unique plant formin that functions as a linking protein between microtubules and microfilaments and thus plays important roles in the process of plant cell division.

show abstract

Section: Immunostaining Was Used To Assess Tubulin Localization In Wisupporting

confidence: 64%

The Type IIArabidopsisFormin14 Interacts with Microtubules and Microfilaments to Regulate Cell Division

et al. 2010

View full text Add to dashboard Cite

show abstract

“…[33] For instance, the actin cables of the phragmosome are decorated with the plant-specific microtubule motor KCH, which crosslinks actin filaments to microtubules. [34] Both 28-residue-peptide constructs were able to enter the cells rapidly, but their intracellular distribution differed completely. Whereas the RLB control peptide accumulated in the vacuole and was excluded from the actin cables of the phragmosome (Figure 6), the RBL construct localized in transvacuolar strands and colocalized with the actin cables of the phragmosome.…”

Section: Resultsmentioning

confidence: 99%

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Eggenberger

Mink²,

Wadhwani³

et al. 2010

ChemBioChem

Self Cite

View full text Add to dashboard Cite

The delivery of externally applied macromolecules or nanoparticles into living cells still represents a critically limiting step before the full capabilities of chemical engineering can be explored. Molecular transporters such as cell-penetrating peptides, peptoids, and other mimetics can be used to carry cargo across the cellular membrane, but it is still difficult to find suitable sequences that operate efficiently for any particular type of cell. Here we report that BP100 (KKLFKKILKYL-amide), originally designed as an antimicrobial peptide against plant pathogens, can be employed as a fast and efficient cell-penetrating agent to transport fluorescent test cargoes into the cytosol of walled plant cells. The uptake of BP100 proceeds slightly more slowly than the endocytosis of fluorescent dextranes, but BP100 accumulates more efficiently and to much higher levels (by an order of magnitude). The entry of BP100 can be efficiently blocked by latrunculin B; this suggests that actin filaments are essential to the uptake mechanism. To test whether this novel transporter can also be used to deliver functional cargoes, we designed a fusion construct of BP100 with the actin-binding Lifeact peptide (MGVADLIKKFESISKEE). We demonstrated that the short BP100 could transport the attached 17-residue sequence quickly and efficiently into tobacco cells. The Lifeact construct retained its functionality as it successfully labeled the actin bundles that tether the nucleus in the cell center.

show abstract

“…In Arabidopsis , AtKP1 has been shown to organize the cortical MT array (Ni et al, 2005; Yang et al, 2011), and to regulate mitochondrial functions (Yang et al, 2011). ATK4 and homologs in cotton and rice, possess a Calponin Homology (CH) domain that mediates interaction with F-actin (Tamura et al, 1999; Preuss et al, 2004; Frey et al, 2009; Xu et al, 2009), and could be important for regulating the motor activity and coordinating the activities of MT and actin microfilaments during premitotic nuclear migration (Umezu et al, 2011). Interestingly, the four members of this class in Physcomitrella also contain the CH domain (Figure 13), strongly suggesting that the binding to actin microfilaments is conserved in moss.…”

Section: Resultsmentioning

confidence: 99%

Phylogenetic Analysis of the Kinesin Superfamily from Physcomitrella

Shen¹,

Collatos²,

Bibeau³

et al. 2012

Front. Plant Sci.

View full text Add to dashboard Cite

Kinesins are an ancient superfamily of microtubule dependent motors. They participate in an extensive and diverse list of essential cellular functions, including mitosis, cytokinesis, cell polarization, cell elongation, flagellar development, and intracellular transport. Based on phylogenetic relationships, the kinesin superfamily has been subdivided into 14 families, which are represented in most eukaryotic phyla. The functions of these families are sometimes conserved between species, but important variations in function across species have been observed. Plants possess most kinesin families including a few plant specific families. With the availability of an ever increasing number of genome sequences from plants, it is important to document the complete complement of kinesins present in a given organism. This will help develop a molecular framework to explore the function of each family using genetics, biochemistry, and cell biology. The moss Physcomitrella patens has emerged as a powerful model organism to study gene function in plants, which makes it a key candidate to explore complex gene families, such as the kinesin superfamily. Here we report a detailed phylogenetic characterization of the 71 kinesins of the kinesin superfamily in Physcomitrella. We found a remarkable conservation of families and subfamily classes with Arabidopsis, which is important for future comparative analysis of function. Some of the families, such as kinesins 14s are composed of fewer members in moss, while other families, such as the kinesin 12s are greatly expanded. To improve the comparison between species, and to simplify communication between research groups, we propose a classification of subfamilies based on our phylogenetic analysis.

show abstract

Dynamic Bridges—A Calponin-Domain Kinesin From Rice Links Actin Filaments and Microtubules in Both Cycling and Non-Cycling Cells

Cited by 53 publications

References 41 publications

The Type IIArabidopsisFormin14 Interacts with Microtubules and Microfilaments to Regulate Cell Division

The Type IIArabidopsisFormin14 Interacts with Microtubules and Microfilaments to Regulate Cell Division

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Phylogenetic Analysis of the Kinesin Superfamily from Physcomitrella

Contact Info

Product

Resources

About