Martine J. Smit

The paper designs miniproteins that selectively block or bias chemokine receptor signaling by targeting CCL25, demonstrating their ability to suppress CCR9 and modulate ACKR4 responses.

This study identifies Ephrin B1 as a key mediator of CXCR4 tumorigenic signaling by promoting its intracellular localization and inhibiting surface expression and signaling.

This study shows ACKR3 is released on extracellular vesicles under both basal and ligand-induced conditions, sequestering chemokines and opioid peptides and modulating their signaling.

This study reveals an unconventional activation mechanism of the atypical GPCR ACKR3 using engineered nanobodies and cryo-EM, showing that extracellular pocket volume changes, not microswitch conformational shifts, drive receptor activity.

This study shows ACKR4 is phosphorylated by GRK3 without needing G protein activation, through a unique receptor motif that recruits the kinase directly.

The paper identifies VHH/single-domain antibodies that either block or enhance Siglec-1 ligand binding to sialylated pathogens on dendritic cells.

This study uses inverse agonistic nanobodies to reveal constitutive activity of ACKR3, showing it drives non-canonical signaling and basal cell motility, suggesting therapeutic potential.

The paper shows that US28's Gq/11 signaling from the plasma membrane, not endosomes, primarily drives gene expression related to glioblastoma proliferation and inflammation.

This study shows that disrupting CXCR4 oligomers in lymphoid cancers reduces migration, survival signaling, and tumor growth, while sensitizing cells to venetoclax.

This study identifies an arrestin-independent phosphorylation mechanism that terminates CCR9 signaling, revealing a novel regulatory pathway for GPCR function.