TY - JOUR TI - Quantitative isoform-profiling of highly diversified recognition molecules AU - Schreiner, Dietmar AU - Simicevic, Jovan AU - Ahrné, Erik AU - Schmidt, Alexander AU - Scheiffele, Peter A2 - Barres, Ben VL - 4 PY - 2015 DA - 2015/05/18 SP - e07794 C1 - eLife 2015;4:e07794 DO - 10.7554/eLife.07794 UR - https://doi.org/10.7554/eLife.07794 AB - Complex biological systems rely on cell surface cues that govern cellular self-recognition and selective interactions with appropriate partners. Molecular diversification of cell surface recognition molecules through DNA recombination and complex alternative splicing has emerged as an important principle for encoding such interactions. However, the lack of tools to specifically detect and quantify receptor protein isoforms is a major impediment to functional studies. We here developed a workflow for targeted mass spectrometry by selected reaction monitoring that permits quantitative assessment of highly diversified protein families. We apply this workflow to dissecting the molecular diversity of the neuronal neurexin receptors and uncover an alternative splicing-dependent recognition code for synaptic ligands. KW - alternative splicing KW - SRM KW - MRM KW - synapse KW - neuroligin KW - recognition JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -