Identification of ADAM12S-interacting proteins in HeLa cells

ADAM12 is an A Disintegrin And Metalloproteinases (ADAMs). It is composed of signaling sequence, prodomain, metalloproteinase, disintegrin, cysteine-rich, EGF-like, transmembrane domains, and a cytoplasmic tail. ADAM12 is highly expressed in multiple cancers and is a diagnostic and prognostic biomarker for the proliferation, migration, and invasion of cancer cells. ADAM12 has several isoforms resulted from splicing variants with different subcellular localization and biological functions. Two most important isoforms are the prototype membrane-anchored long isoform ADAM12L and the secreted short isoform ADAM12S. Both of them contain the N-terminal 704 amino acids while their C-termini are different with each other. ADAM12S has extra 34 amino acids at its C-terminus, which replace the 171-amino acid transmembrane and cytoplasmic tail in ADAM12L. In this work, we use immunoprecipitation and quantitative proteomics to identify the interacting proteins of the short form of ADAM12 (ADAM12S).