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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Myosin X

myosin X, Myo10
This gene encodes a member of the myosin superfamily. The protein represents an unconventional myosin; it should not be confused with the conventional non-muscle myosin-10 (MYH10). Unconventional myosins contain the basic domains of conventional myosins and are further distinguished from class members by their tail domains. This gene functions as an actin-based molecular motor and plays a role in integration of F-actin and microtubule cytoskeletons during meiosis. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: Actin, CAN, STEP, Fascin, HAD
Papers using myosin X antibodies
Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors
Patterson Cam et al., In The Journal of Cell Biology, 1990
... Mouse Myo10 cDNA was cloned into EGFP-C1 Vector (Clontech Laboratories, Inc.) ...
Papers on myosin X
miR-340 suppresses cell migration and invasion by targeting MYO10 in breast cancer.
Fang et al., Jiaxing, China. In Oncol Rep, Feb 2016
At the gene level, MYO10 (myosin X), as a direct miR‑340 target gene, mediated the cell migration and invasion.
Specific Myosins Control Actin Organization, Cell Morphology, and Migration in Prostate Cancer Cells.
Peckham et al., Leeds, United Kingdom. In Cell Rep, Jan 2016
We investigated the myosin expression profile in prostate cancer cell lines and found that Myo1b, Myo9b, Myo10, and Myo18a were expressed at higher levels in cells with high metastatic potential.
Headless Myo10 is a regulator of microtubule stability during neuronal development.
Zhu et al., Changchun, China. In J Neurochem, Oct 2015
In this study, we demonstrate that myosin X (Myo10), which is composed of full-length myosin X (fMyo10) and headless myosin X (hMyo10), is important for axon development.
Direct Microtubule-Binding by Myosin-10 Orients Centrosomes toward Retraction Fibers and Subcortical Actin Clouds.
Pellman et al., Boston, United States. In Dev Cell, Sep 2015
Here, we report that the unconventional myosin, Myo10, couples actin-dependent forces from retraction fibers and subcortical actin clouds to centrosomes.
Global Gene Expression Profiling in Omental Adipose Tissue of Morbidly Obese Diabetic African Americans.
Rotimi et al., Bethesda, United States. In J Endocrinol Metab, Jun 2015
Myosin X (MYO10) and transforming growth factor beta regulator 1 (TBRG1) were upregulated.
Myosin-X and disease.
Cheney et al., Chapel Hill, United States. In Exp Cell Res, Jun 2015
Myosin-X (Myo10) is a motor protein best known for its role in filopodia formation.
Myosin X regulates neuronal radial migration through interacting with N-cadherin.
Zhu et al., Changchun, China. In Front Cell Neurosci, 2014
Myosin X (Myo10), an uncharacteristic member of the myosin family, is an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts.
Cargo recognition and cargo-mediated regulation of unconventional myosins.
Zhang et al., Hong Kong, Hong Kong. In Acc Chem Res, 2014
The structures of the MyTH4-FERM tandems from myosin-VIIa and myosin-X in complex with their respective targets reveal that MyTH4 and FERM domains extensively interact with each other forming structural and functional supramodules in both motors and demonstrate that the structurally similar MyTH4-FERM tandems of the two motors display totally different target binding modes.
An overview of tools for the validation of protein NMR structures.
Gutmanas et al., Leicester, United Kingdom. In J Biomol Nmr, 2014
To discuss their relative merits we have applied the tools to two representative examples from the PDB: a small, globular monomeric protein (Staphylococcal nuclease from S. aureus, PDB entry 2kq3) and a small, symmetric homodimeric protein (a region of human myosin-X, PDB entry 2lw9).
Cadherin-dependent filopodia control preimplantation embryo compaction.
Plachta et al., Australia. In Nat Cell Biol, 2013
Moreover, molecular disruption of the filopodia components E-cadherin, α- and β-catenin, F-actin and myosin-X prevents cells from elongating and compacting the embryo.
Headless Myo10 is a negative regulator of full-length Myo10 and inhibits axon outgrowth in cortical neurons.
Cheney et al., Chapel Hill, United States. In J Biol Chem, 2012
headless Myo10 can function as a negative regulator of full-length Myo10 and that the two isoforms of Myo10 have opposing roles in axon outgrowth.
Differential regulation of myosin X movements by its cargos, DCC and neogenin.
Xiong et al., Augusta, United States. In J Cell Sci, 2012
DCC promotes movement of Myo X along basal actin filaments and enhances Myo-X-mediated basal filopodium elongation.
PtdIns (3,4,5) P3 recruitment of Myo10 is essential for axon development.
Zhu et al., Changchun, China. In Plos One, 2011
Myo10 was required for neuronal morphological transition during radial neuronal migration in the developmental neocortex
Myosin-X: a MyTH-FERM myosin at the tips of filopodia.
Cheney et al., Chapel Hill, United States. In J Cell Sci, 2011
Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia.
Filopodia and adhesion in cancer cell motility.
Ivaska et al., Finland. In Cell Adh Migr, 2011
Integrins are cell surface adhesion receptors critically implicated in cell migration and they are transported actively to filopodia tips by an unconventional myosin, myosin-X.
Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain.
Hakoshima et al., Nara, Japan. In Embo J, 2011
Molecular basis by which myosin-X facilitates alternative dual binding to cargos and microtubules.
Phospholipid-dependent regulation of the motor activity of myosin X.
Ikebe et al., Worcester, United States. In Nat Struct Mol Biol, 2011
Myosin X is monomeric and the band 4.1-ezrin-radixin-moesin (FERM) and pleckstrin homology (PH) domains bind to the head intramolecularly, forming an inhibited conformation.
Myosin VI undergoes cargo-mediated dimerization.
Zhang et al., Hong Kong, Hong Kong. In Cell, 2009
The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.
Myosin X regulates netrin receptors and functions in axonal path-finding.
Xiong et al., Augusta, United States. In Nat Cell Biol, 2007
Here, we provide evidence for the involvement of the unconventional myosin X (Myo X) in netrin-1 function. We find that Myo X interacts with the netrin receptor deleted in colorectal cancer (DCC) and neogenin, a DCC-related protein.
A microtubule-binding myosin required for nuclear anchoring and spindle assembly.
Bement et al., Madison, United States. In Nature, 2004
this myosin has a novel and critically important role during meiosis in integrating the F-actin and microtubule cytoskeletons
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