I-proteins - a proposed switch in myotubularin function.

Michael J Clague; Stephen K Dove; Francis A Barr

doi:10.1016/j.tibs.2003.12.005

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I-proteins - a proposed switch in myotubularin function.

Michael J Clague·Stephen K Dove·Francis A Barr

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Abstract

In this article, we consider the functions of the myotubularins - a large family of phosphoinositide 3-phosphatases. By analogy with the phosphatidylinositol 3-phosphatase PTEN (phosphatase and tensin homolog deleted in chromosome ten) and many protein phosphatases, it has been proposed that the primary function of this protein family is to regulate substrate levels, in this case phosphatidylinositol (3)-phosphate. We propose an alternate, or additional, function that is analogous to the G-protein family of phosphatases, which use nucleotide-dependent conformational changes to transduce signals or do mechanical work.

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Endocytosis Enzyme Activation Feedback, Physiological Models, Biological Mutation Phosphatidylinositol Phosphates Phosphoric Monoester Hydrolases Protein Conformation Protein Structure, Tertiary Protein Tyrosine Phosphatases Protein Tyrosine Phosphatases, Non-Receptor Signal Transduction Substrate Specificity Tumor Suppressor Proteins Journal Article Research Support, Non-U.S. Gov't

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Michael J Clague, Stephen K Dove, Francis A Barr. 2004. I-proteins - a proposed switch in myotubularin function.. https://doi.org/10.1016/j.tibs.2003.12.005

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