The EMLs are a conserved family of microtubule-associated proteins (MAPs). The founding member was discovered in sea urchins as a 77-kDa polypeptide that co-purified with microtubules. This protein, termed EMAP for echinoderm MAP, was the major non-tubulin component present in purified microtubule preparations made from unfertilized sea urchin eggs [J. Cell Sci. (1993) 104, 445–450; J. Cell Sci. (1987) 87(Pt 1), 71–84]. Orthologues of EMAP were subsequently identified in other echinoderms, such as starfish and sand dollar, and then in more distant eukaryotes, including flies, worms and vertebrates, where the name of ELP or EML (both for EMAP-like protein) has been adopted [BMC Dev. Biol. (2008) 8, 110; Dev. Genes Evol. (2000) 210, 2–10]. The common property of these proteins is their ability to decorate microtubules. However, whether they are associated with particular microtubule populations or exercise specific functions in different microtubule-dependent processes remains unknown. Furthermore, although there is limited evidence that they regulate microtubule dynamics, the biochemical mechanisms of their molecular activity have yet to be explored. Nevertheless, interest in these proteins has grown substantially because of the identification of EML mutations in neuronal disorders and oncogenic fusions in human cancers. Here, we summarize our current knowledge of the expression, localization and structure of what is proving to be an interesting and important class of MAPs. We also speculate about their function in microtubule regulation and highlight how the studies of EMLs in human diseases may open up novel avenues for patient therapy.
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October 2016
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Alternative splicing of intrinsically disordered segments can rewire protein interaction networks. In this issue, the Biochemical Society’s Colworth Medal winner, M. Madan Babu explores the contribution of intrinsically disordered regions to protein function, cellular complexity and human disease; see pages 1185–1200. [Credit: Guilhem Chalancon, MRC Laboratory of Molecular Biology, Cambridge, UK.]
Review Article|
October 19 2016
EML proteins in microtubule regulation and human disease
Andrew M. Fry;
Andrew M. Fry
1Cancer Research UK Leicester Centre, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 9HN, U.K.
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Laura O'Regan;
Laura O'Regan
1Cancer Research UK Leicester Centre, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 9HN, U.K.
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Jessica Montgomery;
Jessica Montgomery
1Cancer Research UK Leicester Centre, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 9HN, U.K.
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Rozita Adib;
Rozita Adib
1Cancer Research UK Leicester Centre, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 9HN, U.K.
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Richard Bayliss
Richard Bayliss
2Cancer Research UK Leeds Centre, Faculty of Biological Sciences, University of Leeds, Astbury Building, Leeds LS2 9JT, U.K.
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Biochem Soc Trans (2016) 44 (5): 1281–1288.
Article history
Received:
May 23 2016
Revision Received:
June 14 2016
Accepted:
June 15 2016
Citation
Andrew M. Fry, Laura O'Regan, Jessica Montgomery, Rozita Adib, Richard Bayliss; EML proteins in microtubule regulation and human disease. Biochem Soc Trans 15 October 2016; 44 (5): 1281–1288. doi: https://doi.org/10.1042/BST20160125
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