Adam10 site-dependent biology: Keeping control of a pervasive protease

Research output: Contribution to journalReview articlepeer-review


Enzymes, once considered static molecular machines acting in defined spatial patterns and sites of action, move to different intra-and extracellular locations, changing their function. This topological regulation revealed a close cross-talk between proteases and signaling events involving post-translational modifications, membrane tyrosine kinase receptors and G-protein coupled receptors, motor proteins shuttling cargos in intracellular vesicles, and small-molecule messengers. Here, we highlight recent advances in our knowledge of regulation and function of A Disintegrin And Metalloproteinase (ADAM) endopeptidases at specific subcellular sites, or in multimolecular complexes, with a special focus on ADAM10, and tumor necrosis factor-α convertase (TACE/ADAM17), since these two enzymes belong to the same family, share selected substrates and bioactivity. We will discuss some examples of ADAM10 activity modulated by changing partners and subcellular compartmentalization, with the underlying hypothesis that restraining protease activity by spatial segregation is a complex and powerful regulatory tool.

Original languageEnglish
Pages (from-to)4969
JournalInternational Journal of Molecular Sciences
Issue number9
Publication statusPublished - May 1 2021


  • ADAM
  • ADC
  • Cancer
  • Exosomes
  • Immunomodulation
  • Metalloproteinases
  • Signaling
  • Subcellular trafficking
  • Vesicles

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


Dive into the research topics of 'Adam10 site-dependent biology: Keeping control of a pervasive protease'. Together they form a unique fingerprint.

Cite this