Research ResourceBiochemistry

Proximity biotinylation identifies a set of conformation-specific interactions between Merlin and cell junction proteins

See allHide authors and affiliations

Science Signaling  23 Apr 2019:
Vol. 12, Issue 578, eaau8749
DOI: 10.1126/scisignal.aau8749

The Merlin interactome identifies cell junction proteins

Merlin (also called NF2) is a tumor suppressor that associates with lipid rafts and cell junctions. To identify potential Merlin binding partners, Hennigan et al. performed proximity biotinylation assays in murine Schwann cells with wild-type and various mutant forms of Merlin that could not associate with the plasma membrane or were locked in different conformations. Fewer proteins interacted with the form of Merlin that could not associate with the plasma membrane, and some proteins interacted specifically with the closed conformation. Most of the Merlin-proximal proteins were components of or associated with cell junctions and focal adhesions. Among the previously unidentified Merlin-interacting proteins was the tumor suppressor ASPP2 (also called Tp53bp2), which bound directly to the closed conformation. This dataset confirms cell junctions as important sites for Merlin activity and reveals additional binding partners.

View Full Text

Stay Connected to Science Signaling