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Updated: Dec 17, 2025

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Matriptase processing of APLP1 ectodomain alters its homodimerization.

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Matriptase, a protease, directly cleaves amyloid-like protein 1 (APLP1) at arginine 124. This interaction disrupts APLP1 homodimeric interactions, impacting its functions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid precursor protein (APP) processing by secretases produces amyloid beta peptide (Aβ).
  • Matriptase, a serine protease, cleaves APP, influencing Aβ production.
  • Amyloid-like protein 1 (APLP1) is an APP homolog with shared functional similarities.

Purpose of the Study:

  • To investigate the role of matriptase in the processing of amyloid-like protein 1 (APLP1).
  • To determine if matriptase interacts with and cleaves APLP1.

Main Methods:

  • Cellular assays to demonstrate matriptase-APLP1 interaction.
  • Site-directed mutagenesis (Arg124 to Ala) to assess cleavage site.
  • Bioluminescence resonance energy transfer (BRET) assay to study APLP1 homodimeric interactions.

Main Results:

  • Matriptase directly interacts with APLP1.
  • APLP1 is cleaved by matriptase at arginine 124 within its E1 ectodomain.
  • Mutation of Arg124 to Ala prevents matriptase-mediated cleavage of APLP1.
  • Matriptase reduces APLP1 homodimeric interactions.

Conclusions:

  • Matriptase is identified as the first protease to cleave APLP1.
  • Cleavage occurs within the APLP1 dimerization domain.
  • This cleavage may alter functions associated with APLP1 dimer formation.