General receptor for phosphoinositides 1-associated scaffold protein (TAMALIN)

The **general receptor for phosphoinositides 1-associated scaffold protein (TAMALIN)** is a neuronal molecular scaffold protein highly expressed in the brain, especially in the telencephalon[1][2]. TAMALIN contains a leucine zipper, PDZ domain, and a C-terminal PDZ-binding motif, allowing it to interact with diverse binding partners[2][4]. It regulates the trafficking of group I metabotropic glutamate receptors (mGluR1, mGluR5) to the cell surface by switching between autoinhibited and active conformations via its PDZ domain[1][3]. Moreover, TAMALIN (GRASP) anchors multiprotein signaling complexes that control small GTPase crosstalk, particularly by directly bridging cytohesin 2/ARNO and Dock180, which coordinate the activities of Arf6 and Rac1 and facilitate epithelial cell migration in response to growth factors[4]. TAMALIN therefore plays a central role in neuronal signaling, receptor trafficking, and cellular morphological changes, but is not currently a direct therapeutic target or drug receptor.

Other names

TamalinGRASPGRP1-associated scaffold proteinprotein Tamalingeneral receptor for phosphoinositides 1 associated scaffold protein