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Related Experiment Videos

p38 MAPK regulates COPII recruitment.

Lijun Wang1, John M Lucocq

  • 1Division of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dow Street, Dundee, UK.

Biochemical and Biophysical Research Communications
|September 25, 2007
PubMed
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The stress-activated protein kinase p38 MAPK regulates the early secretory pathway by controlling coat protein complex II (COPII) recruitment to ER export sites, impacting cellular protein transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The early secretory pathway is crucial for protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus.
  • Coat protein complex II (COPII) is essential for forming transport vesicles at ER export sites.
  • Regulation of COPII recruitment is vital for efficient protein secretion.

Purpose of the Study:

  • To investigate the regulatory mechanisms controlling COPII recruitment to ER export sites.
  • To determine the role of stress-activated protein kinases in COPII loading.
  • To elucidate the involvement of p38 MAPK in the early secretory pathway.

Main Methods:

  • Utilized permeabilized HeLa cells for in vitro studies.
  • Analyzed cytosols from nocodazole-treated cells to assess COPII loading.

Related Experiment Videos

  • Employed depletion of p38 MAPK alpha and inhibition with SB203580.
  • Investigated the effect of cdc2 inhibition/depletion.
  • Main Results:

    • COPII loading onto ER export sites was inhibited in cytosols from nocodazole-treated HeLa cells.
    • Activation of p38 MAPK (mitogen-activated protein kinase) was observed in these cytosols.
    • Depletion of p38 MAPK alpha or treatment with the p38 MAPK inhibitor SB203580 rescued COPII loading.
    • Inhibition or depletion of cdc2 did not rescue COPII loading.

    Conclusions:

    • p38 MAPK plays a significant role in regulating COPII recruitment to ER export sites.
    • The stress kinase p38 MAPK is a key regulator of the early secretory pathway.
    • These findings reveal a novel regulatory mechanism for protein transport from the ER.