Remodeling of the Golgi structure by ERK signaling

Jen Hsuan Wei, Joachim Seemann

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Emerging evidence suggests that the Golgi functions as a regulatory node for various signaling cascades. Modules of the MAPK pathway are targeted to the Golgi upon stimulation of cells with mitogens. The target for activated ERK on the Golgi membranes is GRASP65, a peripheral membrane protein required for Golgi cisternal stacking. Phosphorylation of GRASP65 at Serine 277 results in a loss of its oligomerization and causes unstacking of Golgi cisternae. This reorganization of the Golgi structure is required for the polarization of the Golgi and the centrosomes towards the leading edge in migrating cells. Preventing GRASP65 phosphorylation with mutants lacking the phosphorylation site blocks Golgi and centrosome orientation. This demonstrates a mechanism for cell polarization involving dynamic remodeling of the Golgi mediated by local phosphorylation of a Golgi protein induced by mitogen signaling.

Original languageEnglish (US)
Pages (from-to)35-36
Number of pages2
JournalCommunicative and Integrative Biology
Issue number1
StatePublished - 2009


  • Centrosome
  • ERK signaling
  • GRASP65
  • Golgi
  • Migration

ASJC Scopus subject areas

  • General Agricultural and Biological Sciences


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