Filamin is essential for shedding of the transmembrane serine protease, epithin

Chungho Kim, Yongcheol Cho, Chan Hee Kang, Moon Gyo Kim, HyoSeon S. Lee, Eun Gyung Cho, Dongeun Park

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Epithin is a type II transmembrane serine protease that exists in a soluble and membrane-bound form. Shedding is thought to be important in regulating its action, but little is known regarding the intracellular events that trigger such shedding. Here, we show that phorbol myristate acetate (PMA) causes the release of epithin. It also causes accumulation of the protein at the site of cell -cell contacts, and this accumulation is dependent on the formation of cortical actin. In addition, we have identified the actin-binding protein, filamin, as the linker between epithin and the actin cytoskeleton. The interaction of epithin and filamin was enhanced by PMA, and epithin was not released from filamin-deficient M2 cells. We also show that the release of epithin does not require its own activity and is blocked by a metalloprotease inhibitor, GM6001. These results show that filamin has an essential role in shedding by linking epithin to the as yet unidentified metalloprotease-shedding enzyme(s).

Original languageEnglish
Pages (from-to)1045-1051
Number of pages7
JournalEMBO Reports
Volume6
Issue number11
DOIs
Publication statusPublished - 2005 Nov 1
Externally publishedYes

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ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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