Title : Sialidase NEU3 dynamically associates to different membrane domains specifically modifying their ganglioside pattern and triggering Akt phosphorylation.

Pub. Date : 2014

PMID : 24925219






4 Functional Relationships(s)
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1 Sialidase NEU3 dynamically associates to different membrane domains specifically modifying their ganglioside pattern and triggering Akt phosphorylation. Gangliosides neuraminidase 3 Homo sapiens
2 Sialidase NEU3 shows high enzymatic specificity toward gangliosides. Gangliosides neuraminidase 3 Homo sapiens
3 By means of inducible expression cell system we found that i) newly synthesized NEU3 is initially associated to non-DRM; ii) at steady state the protein is equally distributed between the two membrane subcompartments, i.e., DRM and non-DRM; iii) NEU3 is degraded via the proteasomal pathway; iv) the enzyme specifically modifies the ganglioside composition of the membrane areas where it resides; and v) NEU3 triggers phosphorylation of Akt, even in absence of exogenously administered EGF. Gangliosides neuraminidase 3 Homo sapiens
4 Taken together our data demonstrate that NEU3 regulates the DRM ganglioside content and it can be considered as a modulator of Akt phosphorylation, further supporting the role of this enzyme in cancer and tumorigenesis. Gangliosides neuraminidase 3 Homo sapiens