p38 MAPK regulates COPII recruitment

Lijun Wang, John M. Lucocq

    Research output: Contribution to journalArticle

    6 Citations (Scopus)

    Abstract

    Here, we investigate regulation of coat protein complex II (COPII) recruitment onto ER export sites in permeabilized cells. In cytosols from nocodazole treated HeLa cells we find COPII loading is inhibited. The stress kinase p38 MAPK is activated in these cytosols and COPII loading can be rescued by depletion of p38 MAPK alpha or by the p38 MAPK inhibitor (SB203580) but not by inhibition/depletion of cdc2. These observations indicate regulation of the early secretory pathway by p38 MAPK.
    Original languageEnglish
    Pages (from-to)317-21
    Number of pages5
    JournalBiochemical and Biophysical Research Communications
    Volume363
    Issue number2
    DOIs
    Publication statusPublished - 16 Nov 2007

    Fingerprint

    p38 Mitogen-Activated Protein Kinases
    Cytosol
    Nocodazole
    Secretory Pathway
    Capsid Proteins
    HeLa Cells
    Phosphotransferases

    Keywords

    • COP-Coated Vesicles
    • Endoplasmic Reticulum
    • HeLa Cells
    • Humans
    • p38 Mitogen-Activated Protein Kinases

    Cite this

    Wang, Lijun ; Lucocq, John M. / p38 MAPK regulates COPII recruitment. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 363, No. 2. pp. 317-21.
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    p38 MAPK regulates COPII recruitment. / Wang, Lijun; Lucocq, John M.

    In: Biochemical and Biophysical Research Communications, Vol. 363, No. 2, 16.11.2007, p. 317-21.

    Research output: Contribution to journalArticle

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    AU - Wang, Lijun

    AU - Lucocq, John M.

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    KW - Endoplasmic Reticulum

    KW - HeLa Cells

    KW - Humans

    KW - p38 Mitogen-Activated Protein Kinases

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