The extra-cellular signal regulated kinases ERK1 and ERK2 segregate displaying distinct spatiotemporal characteristics in activated mast cells

Anat Benado Bar-Gill, Adi Efergan, Rony Seger, Mitsunori Fukuda, Ronit Sagi-Eisenberg

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    ERK1 and ERK2 are highly homologous isoforms that often play redundant roles in regulating cellular functions. We analyzed the spatiotemporal patterns of ERK1 and ERK2 in resting and activated mast cells. Strikingly, we identified distinct pathways for these kinases. ERK1 localized to the cytosol and translocated to the nucleus upon cell activation and kinase phosphorylation. In contrast, ERK2 distributed between the cytosol and near the microtubule organizing center (MTOC) in resting cells and accumulated further at a pericentrosomal region upon cell trigger. Pericentrosomal accumulation of ERK2 was phosphorylation independent, required an intact microtubule network and was significantly enhanced by the overexpression of Neuronal Calcium Sensor-1 (NCS-1). We also identified γ-tubulin and phosphatidylinositol 4 kinaseβ (PI4Kβ), a downstream effector of NCS-1, as novel partner proteins of ERK2. Taken together, our results imply non-redundant functions of ERK1 and ERK2 in mast cells and implicate NCS-1 and PI4Kβ as regulators of ERK2 trafficking.

    Original languageEnglish
    Pages (from-to)2070-2082
    Number of pages13
    JournalBiochimica et Biophysica Acta - Molecular Cell Research
    Volume1833
    Issue number9
    DOIs
    Publication statusPublished - 2013

    Keywords

    • ERK1
    • ERK2
    • Mast cell
    • NCS-1
    • PI4Kβ
    • Tubulin

    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology

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