Disruption of TACE-filamin interaction can inhibit TACE-mediated ectodomain shedding

Yongcheol Cho, Dongeun Park, Chungho Kim

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Ectodomain shedding regulates functions of many membrane proteins through the cleavage of their juxtamembrane region mainly by a disintegrin and metalloproteinase family proteinases. Tumor necrosis factor-alpha converting enzyme (TACE) is known to be responsible for phorbol myristate acetate (PMA)-induced shedding of various membrane proteins. How PMA regulates TACE-dependent shedding and how TACE exhibits substrate specificity without proteolysis of other membrane proteins are questionable. Here, we show that TACE can interact with an actin-binding protein, filamin, through 20th filamin repeat. We found that the interaction between TACE and filamin was increased by PMA treatment. In addition, loss of filamin or specific disruption of TACE-filamin interaction inhibited ectodomain shedding of representative TACE substrates, CD44 and amyloid protein precursor. From these data, we suggest that filamin may work as a scaffold that can recruit TACE and its substrates in a PMA-dependent manner to achieve substrate specificity for TACE.

Original languageEnglish
Pages (from-to)997-1003
Number of pages7
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2017 Aug 26

Bibliographical note

Publisher Copyright:
© 2017 Elsevier Inc.


  • Ectodomain shedding
  • Epithin
  • Filamin
  • PMA
  • TACE

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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