It takes two to tango: using the ubiquitin fold to turn on secretion

A novel ubiquitin-like domain in protein kinase D (PKD) mediates its dimerisation. Interface residues are depicted in orange and yellow. (c) Thomas Leonard

Protein Kinase D (PKD) is an enzyme at the heart of many cellular functions. By modifying other proteins, it controls the trafficking of essential cargo in the sorting center of the cell, the Golgi apparatus. During his PhD in Thomas Leonard’s lab, Daniel Elsner has identified a ubiquitin-like domain in PKD that plays a crucial role in its activation. The findings, published in the Journal of Biological Chemistry, revise our understanding of how the “on-switch” of PKD is wired in the cell.

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