Myosin Vb localises to nucleoli and associates with the RNA polymerase I transcription complex

Lindsay, Andrew J.; McCaffrey, Mary W.

doi:10.1002/cm.20408

Cited by 35 publications

(27 citation statements)

References 84 publications

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“…MYO5B is ubiquitously expressed, whereas MYO5C is expressed mainly in glandular and epithelial cells [84]. However both proteins were selectively expressed in the NEC cell lines, suggesting specific function in epithelial-like cells.…”

Section: Resultsmentioning

confidence: 96%

Gene Expression Correlations in Human Cancer Cell Lines Define Molecular Interaction Networks for Epithelial Phenotype

et al. 2014

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Using gene expression data to enhance our knowledge of control networks relevant to cancer biology and therapy is a challenging but urgent task. Based on the premise that genes that are expressed together in a variety of cell types are likely to functions together, we derived mutually correlated genes that function together in various processes in epithelial-like tumor cells. Expression-correlated genes were derived from data for the NCI-60 human tumor cell lines, as well as data from the Broad Institute’s CCLE cell lines. NCI-60 cell lines that selectively expressed a mutually correlated subset of tight junction genes served as a signature for epithelial-like cancer cells. Those signature cell lines served as a seed to derive other correlated genes, many of which had various other epithelial-related functions. Literature survey yielded molecular interaction and function information about those genes, from which molecular interaction maps were assembled. Many of the genes had epithelial functions unrelated to tight junctions, demonstrating that new function categories were elicited. The most highly correlated genes were implicated in the following epithelial functions: interactions at tight junctions (CLDN7, CLDN4, CLDN3, MARVELD3, MARVELD2, TJP3, CGN, CRB3, LLGL2, EPCAM, LNX1); interactions at adherens junctions (CDH1, ADAP1, CAMSAP3); interactions at desmosomes (PPL, PKP3, JUP); transcription regulation of cell-cell junction complexes (GRHL1 and 2); epithelial RNA splicing regulators (ESRP1 and 2); epithelial vesicle traffic (RAB25, EPN3, GRHL2, EHF, ADAP1, MYO5B); epithelial Ca(+2) signaling (ATP2C2, S100A14, BSPRY); terminal differentiation of epithelial cells (OVOL1 and 2, ST14, PRSS8, SPINT1 and 2); maintenance of apico-basal polarity (RAB25, LLGL2, EPN3). The findings provide a foundation for future studies to elucidate the functions of regulatory networks specific to epithelial-like cancer cells and to probe for anti-cancer drug targets.

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Section: Resultsmentioning

confidence: 96%

Gene Expression Correlations in Human Cancer Cell Lines Define Molecular Interaction Networks for Epithelial Phenotype

et al. 2014

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“…Antibodies-Rabbit polyclonal antibodies to myosin Va (LF-18) and Dcp1a (HPA013202), mouse monoclonal anti-␣ tubulin, and chicken anti-Lsm1 were from Sigma-Aldrich. Rabbit polyclonal anti-myosin Vb has been described elsewhere (17). Mouse monoclonal anti-eIF4E (product P-2) and goat anti-TIA-1 (product C-20) were from Santa Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

Myosin Va Is Required for P Body but Not Stress Granule Formation

Lindsay

McCaffrey

2011

Journal of Biological Chemistry

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In the present study we demonstrate an association between mammalian myosin Va and cytoplasmic P bodies, microscopic ribonucleoprotein granules that contain components of the 5-3 mRNA degradation machinery. Myosin Va colocalizes with several P body markers and its RNAi-mediated knockdown results in the disassembly of P bodies. Overexpression of a dominant-negative mutant of myosin Va reduced the motility of P bodies in living cells. Co-immunoprecipitation experiments demonstrate that myosin Va physically associates with eIF4E, an mRNA binding protein that localizes to P bodies. In contrast, we find that myosin Va does not play a role in stress granule formation. Stress granules are ribonucleoprotein structures that are involved in translational silencing and are spatially, functionally, and compositionally linked to P bodies. Myosin Va is found adjacent to stress granules in stressed cells but displays minimal localization within stress granules, and myosin Va knockdown has no effect on stress granule assembly or disassembly. Combined with recently published reports demonstrating a role for Drosophila and mammalian class V myosins in mRNA transport and the involvement of the yeast myosin V orthologue Myo2p in P body assembly, our results provide further evidence that the class V myosins serve an important role in the transport and turnover of mRNA.Class V myosins are actin-based motor proteins composed of two identical heavy chains and several associated light chains. The amino-terminal head domain binds to ATP and actin filaments and provides the motive force for the complex. The neck region contains six calmodulin binding IQ motifs and acts as a lever arm, whereas the carboxyl-terminal tail domain mediates binding to cargo (1). Yeast have two class V myosins, flies and worms have one, whereas mammals have three (Va, Vb, and Vc). Myosin Va (MyoVa) 2 is widely expressed but is enriched in brain, testes, and skin. It has been implicated in a diverse range of cellular roles, including synaptic vesicle transport (2), insulin secretion (3), myelination (4), and long term potentiation (5). People who lack functional myosin Va suffer from a rare autosomal recessive disorder called Griscelli syndrome, which is characterized by hypopigmentation and severe neurological defects (6).It is well established that the yeast class V myosin Myo4p actively transports Ash1 mRNA to the bud tip of dividing cells (7), but it is now emerging that class V myosins from higher eukaryotes also play roles in RNA transport. Myosin Va has been found associated with several RNA binding proteins in a messenger ribonucleoprotein (mRNP) complex precipitated from a mouse brain extract (8). The intracellular distribution of RNA is dramatically altered in primary cells derived from dilute-lethal (myosin Va-null) mice (9). Yoshimura et al. (10) have shown that myosin Va mediates the translocation of TLS (translated in liposarcoma) and its target RNA, Nd1-L, into dendritic spines, and myosin V is involved in targeting oskar mRNA to the posterior po...

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“…The inhibition of transcription in HeLa cells caused by actinomycin D motivate myosin Va phosphorylation and cause the redistribution of myosin Va to nucleoli [230]. Nevertheless, myosin Vb is present in nucleolus, and this protein interacts with actin, RNA polymerase I and newly transcribed ribosomal RNA [231]. The roles of myosin Vb in transcription process have attracted the interest of scientists.…”

Section: A New Concept Of “Chromomyosin”mentioning

confidence: 99%

Myosins as fundamental components during tumorigenesis: diverse and indispensable

Yang

2016

Oncotarget

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Myosin is a kind of actin-based motor protein. As the crucial functions of myosin during tumorigenesis have become increasingly apparent, the profile of myosin in the field of cancer research has also been growing. Eighteen distinct classes of myosins have been discovered in the past twenty years and constitute a diverse superfamily. Various myosins share similar structures. They all convert energy from ATP hydrolysis to exert mechanical stress upon interactions with microfilaments. Ongoing research is increasingly suggesting that at least seven kinds of myosins participate in the formation and development of cancer. Myosins play essential roles in cytokinesis failure, chromosomal and centrosomal amplification, multipolar spindle formation and DNA microsatellite instability. These are all prerequisites of tumor formation. Subsequently, myosins activate various processes of tumor invasion and metastasis development including cell migration, adhesion, protrusion formation, loss of cell polarity and suppression of apoptosis. In this review, we summarize the current understanding of the roles of myosins during tumorigenesis and discuss the factors and mechanisms which may regulate myosins in tumor progression. Furthermore, we put forward a completely new concept of “chromomyosin” to demonstrate the pivotal functions of myosins during karyokinesis and how this acts to optimize the functions of the members of the myosin superfamily.

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Myosin Vb localises to nucleoli and associates with the RNA polymerase I transcription complex

Cited by 35 publications

References 84 publications

Gene Expression Correlations in Human Cancer Cell Lines Define Molecular Interaction Networks for Epithelial Phenotype

Gene Expression Correlations in Human Cancer Cell Lines Define Molecular Interaction Networks for Epithelial Phenotype

Myosin Va Is Required for P Body but Not Stress Granule Formation

Myosins as fundamental components during tumorigenesis: diverse and indispensable

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