Myosin‐Va mediates RNA distribution in primary fibroblasts from multiple organs

Salerno, Verônica P.; Calliari, Aldo; Provance, David William; Sotelo‐Silveira, José; Sotelo, Julio; Mercer, John A.

doi:10.1002/cm.20272

Cited by 25 publications

(21 citation statements)

References 44 publications

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“…Multiple functions have been assigned to this actin-dependent molecular motor, including the transport of melanosomes, smooth endoplasmic reticulum, recycling endosomes, neurotransmitter vesicles, mRNA (Reck-Peterson et al 2000, Langford 2002, Salerno et al 2008, and neuroendocrine vesicles (Rudolf et al 2003). A role for MYO5A in tumor cell migration, invasion, and metastasis has recently been described (Du et al 2007, Lan et al 2010.…”

Section: Discussionmentioning

confidence: 99%

Differential gene expression profiles of invasive and non-invasive non-functioning pituitary adenomas based on microarray analysis

Galland¹,

Lacroix²,

Saulnier³

et al. 2010

Endocrine-Related Cancer

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Non-functioning pituitary adenomas (NFPAs) may be locally invasive. Markers of invasiveness are needed to guide patient management and particularly the use of adjuvant radiotherapy. To examine whether invasive NFPAs display a specific gene expression profile relative to non-invasive tumors, we selected 40 NFPAs (38 of the gonadotroph type) and classified them as invasive (nZ22) or non-invasive (nZ18) on the basis of magnetic resonance imaging and surgical findings. We then performed pangenomic analysis with the 44k Agilent human whole genome expression oligonucleotide microarray in order to identify genes with differential expression between invasive and non-invasive NFPAs. Candidate genes were then tested in qRT-PCR. Prediction class analysis showed that the expression of 346 genes differed between invasive and non-invasive NFPAs (P!0.001), of which 233 genes were up-regulated and 113 genes were down-regulated in invasive tumors. On the basis of Ingenuity networks and the degree of up-or down-regulation in invasive versus non-invasive tumors, 35 genes were selected for expression quantification by qRT-PCR. Overexpression of only four genes was confirmed, namely IGFBP5 (PZ0.02), MYO5A (PZ0.04), FLT3 (PZ0.01), and NFE2L1 (PZ0.02). At the protein level, only myosin 5A (MYO5A) immunostaining was stronger in invasive than in non-invasive NFPAs. Molecular signature allows to differentiate 'grossly' invasive from non-invasive NFPAs. The product of one of these genes, MYO5A, may be a useful marker of tumor invasiveness.

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Section: Discussionmentioning

confidence: 99%

Differential gene expression profiles of invasive and non-invasive non-functioning pituitary adenomas based on microarray analysis

Galland¹,

Lacroix²,

Saulnier³

et al. 2010

Endocrine-Related Cancer

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“…It could be proposed therefore that directed ZBP1 transport is carried out by and requires a fine-tuned regulation of multiple microtubule and actin motors. Myosin Va (MyoVa) is a fast processive myosin that transports diverse cargoes such as vesicles (Kogel et al, 2010; Wu et al, 1997), neurofilaments (Rao et al, 2002), mitochondria (Pathak et al, 2010) and ER (Wagner et al, 2011), as well as RNA (Krauss et al, 2009; Salerno et al, 2008; Yoshimura et al, 2006). Mutations of MyoVa cause Griscelli syndrome in humans and dilute-lethal phenotype in mice, which display defects in skin/coat color and have neurological phenotypes (Pastural et al, 1997; Takagishi and Murata, 2006).…”

Section: Introductionmentioning

confidence: 99%

Regulation of Zipcode Binding Protein 1 Transport Dynamics in Axons by Myosin Va

et al. 2012

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Directed transport of the mRNA binding protein, zipcode binding protein1 (ZBP1), into developing axons is believed to play an important role in mRNA localization and local protein synthesis. The role of molecular motors in this process is unclear. We elucidated a role for Myosin Va (MyoVa) to modulate the axonal localization and transport of ZBP1 in axons. Using cultured rat hippocampal neurons, ZBP1 colocalized with MyoVa in axons and growth cones. Interaction of MyoVa with ZBP1 was evident by co-immunoprecipitation of endogenous and overexpressed proteins. Inhibition of MyoVa function with the globular tail domain (GTD) of MyoVa protein or short hairpin RNA led to an accumulation of ZBP1 in axons. Live cell imaging of mCherryZBP1 in neurons expressing GTD showed an increase in the number of motile particles, run length and stimulated anterograde moving ZBP1 particles, suggesting that MyoVa controls availability of ZBP1 for microtubule-dependent transport. These findings suggest a novel regulatory role for MyoVa in the transport of ZBP1 within axons.

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“…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 pole of the Drosophila oocyte (11).…”

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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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Myosin‐Va mediates RNA distribution in primary fibroblasts from multiple organs

Cited by 25 publications

References 44 publications

Differential gene expression profiles of invasive and non-invasive non-functioning pituitary adenomas based on microarray analysis

Differential gene expression profiles of invasive and non-invasive non-functioning pituitary adenomas based on microarray analysis

Regulation of Zipcode Binding Protein 1 Transport Dynamics in Axons by Myosin Va

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

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