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Two membrane proteins that belong to a new type of cell-surface receptor mediate the transmembrane signaling for a secreted factor that has broad therapeutic value.

Structural, biophysical and physiological analysis reveals how yeast cell surface adhesins evolved to confer self-nonself discrimination in single cells and whole populations.

Cells control the spatial organization and signaling of TGFβ receptors at focal adhesions via a mechanically regulated mechanism to integrate biochemical and physical cues.

A proteo-genomic CRISPR activation screening workflow to accelerate the identification of novel interactions between the secreted and membrane proteome with the potential to define new biological processes and identify future therapeutic targets.

Combining particle tracking in living cells with statistical analysis demonstrates how the oligomeric organization of cell surface receptor influences their function, a necessary step in the development of drugs targeting specific receptor conformation.

GDE3 is a transmembrane GPI-specific phospholipase C that sheds the urokinase receptor (uPAR) from the cell surface resulting in loss of uPAR function in breast cancer cells and reduced tumor growth.

IRS-1, a canonical signaling mediator of IGF-I receptor, serves as an endocytic regulator of IGF-I receptor to facilitate the sustained IGF signaling.

Although genetically and biochemically linked, the plant immune and growth receptors FLS2 and BRI1 form dispersed receptor clusters within the plasma membrane that are spatiotemporally separated.

Enigmatic long-lived plasma cells display an enhanced clustering in bone marrow niches and require CXCR4 for retention, survival, and maintenance of antibody titers.

FERONIA receptor kinase interacts with phosphatidylinositol-anchored proteins LORELEI and LLG1 to ensure its proper functional location in the cell membrane and engages them as co-receptors on the cell surface to mediate a broad spectrum of growth and signaling processes.