Biotinylation by antibody recognition - a method for proximity labeling

Daniel Z. Bar, Kathleen Atkatsh, Urraca Tavarez, Michael R. Erdos, Yosef Gruenbaum, Francis S. Collins*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The high-throughput detection of organelle composition and proteomic mapping of protein environment directly from primary tissue as well as the identification of interactors of insoluble proteins that form higher-order structures have remained challenges in biological research. We report a proximity-based labeling approach that uses an antibody to a target antigen to guide biotin deposition onto adjacent proteins in fixed cells and primary tissues, which allows proteins in close proximity to the target antigen to be captured and identified by mass spectrometry. We demonstrated the specificity and sensitivity of our method by examining the well-studied mitochondrial matrix. We then used the method to profile the dynamic interactome of lamin A/C in multiple cell and tissue types under various treatment conditions. The ability to detect proximal proteins and putative interactors in intact tissues, and to quantify changes caused by different conditions or in the presence of disease mutations, can provide a window into cell biology and disease pathogenesis.

Original languageEnglish
Pages (from-to)127-133
Number of pages7
JournalNature Methods
Issue number2
StatePublished - 1 Feb 2018
Externally publishedYes


Dive into the research topics of 'Biotinylation by antibody recognition - a method for proximity labeling'. Together they form a unique fingerprint.

Cite this