Dataset Information

Quantitative isoform-profiling of highly diversified recognition molecules.

ABSTRACT: 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.

SUBMITTER: Schreiner D

PROVIDER: S-EPMC4489214 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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Quantitative isoform-profiling of highly diversified recognition molecules.

Schreiner Dietmar D Simicevic Jovan J Ahrné Erik E Schmidt Alexander A Scheiffele Peter P

eLife 20150518

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 ...[more]

PMID: 25985086

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Dataset Information

Quantitative isoform-profiling of highly diversified recognition molecules.

Publications

Quantitative isoform-profiling of highly diversified recognition molecules.

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