Phosphorylation of Plant Microtubule-Associated Proteins During Cell Division

Abstract

Progression of mitosis and cytokinesis depends on the reorganization of cytoskeleton, with microtubules driving the segregation of chromosomes and their partitioning to two daughter cells. In dividing plant cells, microtubules undergo global reorganization throughout mitosis and cytokinesis, and with the aid of various microtubule-associated proteins (MAPs), they form unique systems such as the preprophase band (PPB), the acentrosomal mitotic spindle, and the phragmoplast. Such proteins include nucleators of de novo microtubule formation, plus end binding proteins involved in the regulation of microtubule dynamics, crosslinking proteins underlying microtubule bundle formation and members of the kinesin superfamily with microtubule-dependent motor activities. The coordinated function of such proteins not only drives the continuous remodeling of microtubules during mitosis and cytokinesis but also assists the positioning of the PPB, the mitotic spindle, and the phragmoplast, affecting tissue patterning by controlling cell division plane (CDP) orientation. The affinity and the function of such proteins is variably regulated by reversible phosphorylation of serine and threonine residues within the microtubule binding domain through a number of protein kinases and phosphatases which are differentially involved throughout cell division. The purpose of the present review is to provide an overview of the function of protein kinases and protein phosphatases involved in cell division regulation and to identify cytoskeletal substrates relevant to the progression of mitosis and cytokinesis and the regulation of CDP orientation.

Tubulin Acetylation Mediates Bisphenol A Effects on the Microtubule Arrays of Allium cepa and Triticum turgidum

“…More recently, it has been found that BPA resulted in a mis-localization of MAPs, leading to a failure of spindle attachment on the kinetochores [20]. In our experiments, the contact of microtubules to kinetochores also seemed to be disrupted (Figure 4), so a reasonable assumption could be that BPA perturbed MAP localization also in plant cells, which is vital for spindle microtubule attachment to kinetochores [48]—a hypothesis deserving further confirmation.…”

In Silico Characterization of a Cyclin Dependent Kinase -A (CDKA) and its Coding Gene in some Oryza Species

“…In nucleus, CDKA is involved in DNA replication (36) and formation of synaptonemal complex at the beginning of meiosis (18). In cytoplasm, CDKA is associated with spindle (37,38) and phragmoplast formation (39 Analyses of the amino acid sequences of CDKA mined from the studied Oryza genomes showed 291-292 amino acid length in all species except O. longistaminata that appeared as a shorter amino acid chain of 273 residues (Fig. 3).…”

Plant Kinesin-12: Localization Heterogeneity and Functional Implications

“…Alternatively, kinesin-12 themselves might be direct substrates of the NACK-PQR MAPK signaling components. It is worthwhile mentioning that recently POK2/Kin12D was predicted as a putative target of AURORA kinase [43]. AURORAs are localizing to the phragmoplast [44,45] although the prediction was related to the cortical division zone targeting (see below) of POK2/Kin12D.…”