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ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease

期刊

出版社

MDPI
DOI: 10.3390/ijms22094969

关键词

ADAM; metalloproteinases; subcellular trafficking; vesicles; exosomes; signaling; cancer; ADC; immunomodulation

资金

  1. 5x1000 2015 from the Italian Ministry of Health
  2. 5x1000 2016 from the Italian Ministry of Health
  3. AIRC (Associazione Italiana per la Ricerca sul Cancro) [IG-21648 28/11/2018]

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Enzymes are no longer considered static molecular machines, as they can move to different locations and change their functions. Recent research focuses on the regulation and function of ADAM endopeptidases at specific subcellular sites or in multimolecular complexes, particularly ADAM10 and TACE/ADAM17.
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-alpha 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.

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