Caprice/<scp>MISP</scp> is a novel <scp>F</scp>‐actin bundling protein critical for actin‐based cytoskeletal reorganizations

Kumeta, Masahiro; Gilmore, Jamie L.; Umeshima, Hiroki; Ishikawa, Masaaki; Horigome, Tsuneyoshi; Kengaku, Mineko

doi:10.1111/gtc.12131

Cited by 18 publications

(26 citation statements)

References 32 publications

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“…Interestingly, recent studies from independent groups have shown that MISP is required for spindle positioning and accurate chromosome segregation, and that phostphorylation of MISP is critical for its function (Maier et al, ; Nain and Cimini, ; Zhu et al, ). Moreover, this protein was also found to be an actin‐binding protein (Kumeta et al, ), which is consistent with our observation that NUP88 associates with MISP in the insoluble fraction (Fig. A).…”

Section: Resultssupporting

confidence: 92%

Multiple biological processes may be associated with tumorigenesis under NUP88‐overexpressed condition

Zhao

2016

Genes Chromosomes & Cancer

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Overexpression of the nucleoporin NUP88 has been observed in a large number of tumors and has been experimentally proven to promote tumorigenesis. However, the mechanism underlying the tumor-promoting activity of overexpressed NUP88 is not clear. To investigate the potential pathways that drive tumorigenesis under NUP88 overexpressed condition, we applied a proteomic approach to identify NUP88-associated proteins at a subcellular compartment level. Gene ontology analysis revealed significant associations between NUP88 interactome and biological processes that are related to nuclear transport, RNA processing, cell cycle progression, metabolic regulation, and viral infection. Moreover, we found that NUP88 interacts with MISP, a mitotic interactor and substrate of PLK1. Interestingly, NUP88 overexpression blocks MISP phosphorylation, which is known to be critical for normal spindle formation and accurate chromosome segregation during mitosis. In conclusion, our data for the first time provide a global view of biological processes that may drive tumorigenesis under NUP88 overexpressed condition, revealing a biological effect of NUP88-MISP interaction. Furthermore, identification of NUP88-associated proteins provides a valuable database for future studies. © 2016 Wiley Periodicals, Inc.

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Section: Resultssupporting

confidence: 92%

Multiple biological processes may be associated with tumorigenesis under NUP88‐overexpressed condition

Zhao

2016

Genes Chromosomes & Cancer

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“…Importantly, our studies show that MISP is strongly associated with actin in polarized cells ( Fig. S1D), which is similar to what was described in non-polarized cells (Maier et al, 2013;Zhu et al, 2013;Kumeta et al, 2014). Interestingly, MISP and ezrin partially colocalize in polarized cells at the apical cortex (Fig.…”

Section: Activated Ezrin Interacts With Misp At the Cell Cortexsupporting

confidence: 87%

“…The recently identified unstructured protein mitotic interactor and substrate of Plk1 (MISP) is strongly associated with actin and is highly phosphorylated during mitosis by Cdk1 and Plk1 (Maier et al, 2013;Zhu et al, 2013;Kumeta et al, 2014). MISP localizes at the cell cortex throughout the cell cycle and contributes to proper cortical distribution of p150 glued (also known as DCTN1), astral MT stability and correct mitotic spindle placement (Zhu et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Activated ezrin controls MISP levels to ensure correct NuMA polarization and spindle orientation

Kschonsak

Hoffmann

2018

Journal of Cell Science

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Correct spindle orientation is achieved through signaling pathways that provide a molecular link between the cell cortex and spindle microtubules in an F-actin-dependent manner. A conserved cortical protein complex, composed of LGN (also known as GPSM2), NuMA (also known as NUMA1) and dynein-dynactin, plays a key role in establishing proper spindle orientation. It has also been shown that the actin-binding protein MISP and the ERM family, which are activated by lymphocyte-oriented kinase (LOK, also known as STK10) and Ste20-like kinase (SLK) (hereafter, SLK/LOK) in mitosis, regulate spindle orientation. Here, we report that MISP functions downstream of the ERM family member ezrin and upstream of NuMA to allow optimal spindle positioning. We show that MISP directly interacts with ezrin and that SLK/LOK-activated ezrin ensures appropriate cortical MISP levels in mitosis by competing with MISP for actin-binding sites at the cell cortex. Furthermore, we found that regulation of the correct cortical MISP levels, by preventing its excessive accumulation, is essential for crescent-like polarized NuMA localization at the cortex and, as a consequence, leads to highly dynamic astral microtubules. Our results uncover how appropriate MISP levels at the cortex are required for proper NuMA polarization and, therefore, an optimal placement of the mitotic spindle within the cell.This article has an associated First Person interview with the first author of the paper.

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“…Studies in keratin 17-null mice uncovered several roles including resistance to TNFα-induced apoptosis [30] . MISP functions as a single actin-binding effector of cell morphology [31] and could be related to the morphological modifications of the apoptotic cell. The results suggest a concerted role of these genes in apoptosis after the ER stress in mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

Identification of stress responsive genes by studying specific relationships between mRNA and protein abundance

Morimoto

Yahara

2018

Heliyon

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Protein expression is regulated by the production and degradation of mRNAs and proteins but the specifics of their relationship are controversial. Although technological advances have enabled genome-wide and time-series surveys of mRNA and protein abundance, recent studies have shown paradoxical results, with most statistical analyses being limited to linear correlation, or analysis of variance applied separately to mRNA and protein datasets. Here, using recently analyzed genome-wide time-series data, we have developed a statistical analysis framework for identifying which types of genes or biological gene groups have significant correlation between mRNA and protein abundance after accounting for potential time delays. Our framework stratifies all genes in terms of the extent of time delay, conducts gene clustering in each stratum, and performs a non-parametric statistical test of the correlation between mRNA and protein abundance in a gene cluster. Consequently, we revealed stronger correlations than previously reported between mRNA and protein abundance in two metabolic pathways. Moreover, we identified a pair of stress responsive genes (ADC17 and KIN1) that showed a highly similar time series of mRNA and protein abundance. Furthermore, we confirmed robustness of the analysis framework by applying it to another genome-wide time-series data and identifying a cytoskeleton-related gene cluster (keratin 18, keratin 17, and mitotic spindle positioning) that shows similar correlation. The significant correlation and highly similar changes of mRNA and protein abundance suggests a concerted role of these genes in cellular stress response, which we consider provides an answer to the question of the specific relationships between mRNA and protein in a cell. In addition, our framework for studying the relationship between mRNAs and proteins in a cell will provide a basis for studying specific relationships between mRNA and protein abundance after accounting for potential time delays.

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Caprice/MISP is a novel F‐actin bundling protein critical for actin‐based cytoskeletal reorganizations

Cited by 18 publications

References 32 publications

Multiple biological processes may be associated with tumorigenesis under NUP88‐overexpressed condition

Multiple biological processes may be associated with tumorigenesis under NUP88‐overexpressed condition

Activated ezrin controls MISP levels to ensure correct NuMA polarization and spindle orientation

Identification of stress responsive genes by studying specific relationships between mRNA and protein abundance

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