An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

Publication

Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.

Bartolec TK, Vazquez-Campos X, Norman A, Luong C, Johnson M, Payne RJ, Wilkins MR, Mackay JP, Low JKK

Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking ... [more]

Proc Natl Acad Sci U S A Apr. 25, 2023; 120(17);e2219418120 [Pubmed: 37071682]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
ACTA2 TPM1	Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.	Havugimana PC (2012)	High	0.763	BioGRID	746479

Curated By

BioGRID

Interaction Summary

TPM1

Gene Ontology Biological Process

Gene Ontology Molecular Function

actin binding [TAS]cytoskeletal protein binding [IPI]structural constituent of cytoskeleton [TAS]structural constituent of muscle [TAS]

Gene Ontology Cellular Component

ACTA2