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    Neurosci Lett. 2009 May 8;455(1):60-4. Epub 2009 Mar 6.

    ELP3 localises to mitochondria and actin-rich domains at edges of HeLa cells.

    Barton D, Braet F, Marc J, Overall R, Gardiner J.

    Source

    The School of Biological Sciences, The University of Sydney, Camperdown, NSW 2006, Australia.

    Abstract

    Motor neuron disease is associated with mutations in the ELP3 protein. Familial dysautonomia is a hereditary disease of the autonomous nervous system that occurs due to a mutation in the IkappaB kinase complex-associated protein (IKAP). Both ELP3 and IKAP are components of the ELONGATOR histone acetylase complex. This complex has six subunits ELP1 (IKAP)-ELP6. ELP3 is the acetylase component of the complex and is known to play a key role in histone acetylation. However, ELONGATOR components including IKAP also localise to cytoplasmic compartments, including actin-rich membrane ruffles. Therefore it is likely that the ELP3 acetylase may also acetylate cytoplasmic proteins. Here, we show using immunofluorescence with two different antibodies against ELP3 that it localises to mitochondria in HeLa cells as well as actin-like filaments and actin-rich sites at the edges of spreading cells. This suggests that ELP3, and possibly the ELONGATOR complex may play a role in mitochondrial function, as well as in actin organisation and cell motility.

    PMID:
    19429107
    [PubMed - indexed for MEDLINE]

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