Definitions

from Wiktionary, Creative Commons Attribution/Share-Alike License.

  • noun biochemistry A phosphatase that dephosphorylates phosphatidylinositols

Etymologies

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Examples

  • We were able to record at precise time points GFP-tagged myotubularin oligomerization in osmotically challenged living cells.

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • To exemplify the accessibility of the method, we characterized the oligomerization of GFP-tagged myotubularin induced by hypo-osmotic treatment at the ultrastructural level.

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • They do not correspond to membrane tubules, as hypothesized from the known function of myotubularin, but represent most likely oligomers, that were previously described Correlative light and electron microscopy of the needle-like structures.

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • We provide examples of the dynamic oligomerization of GFP-tagged myotubularin (MTM1) phosphoinositides phosphatase induced by osmotic stress, and of the ultrastructure of membrane tubules dependent on amphiphysin 2 (BIN1) expression.

    Elites TV 2010

  • Schaletzky J, Dove SK, Short B, Lorenzo O, Clague MJ, et al. (2003) Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases.

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • (A) COS-1 cells were transfected with GFP or YFP-tagged wild-type myotubularin (MTM1) or close homologous proteins MTMR2 and MTMR4, either untreated or switched to a hypo-osmotic medium for

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • We provide examples of the dynamic oligomerization of GFP-tagged myotubularin (MTM1) phosphoinositides phosphatase induced by osmotic stress, and of the ultrastructure of membrane tubules dependent on amphiphysin 2 (BIN1) expression.

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

  • Some PTP members of the PTEN and myotubularin families have evolved to dephosphorylate phosphatidylinositol phosphates specifically

    PLoS ONE Alerts: New Articles 2009

  • The second PTP domain (D2) of many classical receptor-like PTPs and the PTP domain of dual-specificity pseudophosphatases of the myotubularin family lack critical residues essential for their catalytic activity

    PLoS ONE Alerts: New Articles 2009

  • This nucleation is enhanced by the GFP tag, as untagged proteins usually retain normal localization, and is dependent on the myotubularin sequence as the localization of close homologues is not similarly affected (

    PLoS ONE Alerts: New Articles Coralie Spiegelhalter et al. 2010

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