The manganese cation disrupts membrane dynamics along the secretory pathway

Mhairi C. Towler, Alan R. Prescott, John James, John M. Lucocq, Sreenivasan Ponnambalam (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)

Abstract

The endoplasmic reticulum and Golgi apparatus play key roles in regulating the folding, assembly, and transport of newly synthesized proteins along the secretory pathway. We find that the divalent cation manganese disrupts the Golgi apparatus and endoplasmic reticulum (ER). The Golgi apparatus is fragmented into smaller dispersed structures upon manganese treatment. Golgi residents, such as TGN46, β1,4-galactosyltransferase, giantin, and GM130, are still segregated and partitioned correctly into smaller stacked fragments in manganese-treated cells. The mesh-like ER network is substantially affected and peripheral ER elements are collapsed. These effects are consistent with manganese-mediated inhibition of motor proteins that link membrane organelles along the secretory pathway to the cytoskeleton. This divalent cation thus represents a new tool for studying protein secretion and membrane dynamics along the secretory pathway. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)167-179
Number of pages13
JournalExperimental Cell Research
Volume259
Issue number1
DOIs
Publication statusPublished - 25 Aug 2000

Keywords

  • Endoplasmic reticulum
  • Golgi apparatus
  • Manganese
  • Membranes
  • Secretion

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