1. “Topological features of integrin adhesion complexes revealed by multiplexed proximity biotinylation” now out in @JCellBiol. https://is.gd/pp1krb ">https://is.gd/pp1krb&qu...

2. Congrats @MeganChastney Craig Lawless @JDHL18 @DrMCJones33 @BioMS_ManUni @wtccmr @FBMH_UoM. Great collaboration with @claus_jorgensen @CRUK_MI.

3. We used multiplexed proximity biotinylation (BioID – thanks @LabBurke!) to generate an in situ, proximity-dependent adhesome in mouse pancreatic fibroblasts. Integration of the interactomes of 16 baits revealed a network of 147 proteins with 361 proximity interactions.

4. Bioinformatic analysis revealed five clusters of baits (B1-B5) that link to common prey, & which may represent functional modules. B1 contained kindlin-2/ILK/a-parvin/PINCH, B2 FAK/paxillin/p130Cas/vinculin, B3 GIT1/b-Pix, B4 LPP/TRIP6, & B5 palladin/PDLIM5/ponsin/zyxin.

5. The clusters, and their spatial associations, are consistent with current models of integrin adhesion complex (IAC) stratification. This is best exemplified by domain-dependent associations of talin-1 with different baits.

6. The network also revealed a group of 11 highly connected proteins with multiple links to all five bait clusters, which may represent core IAC components. These comprised talin-1/tensins-1 & -3/KANK2/LL5-a/Peak1/PTP-PEST/LIMD1/scribble/erbin/Ppp2r3a (a PP2A regulatory subunit).