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Golgi maturation-dependent glycoenzyme recycling controls glycosphingolipid biosynthesis and cell growth via GOLPH3. 2021
Riccardo Rizzo, and
Domenico Russo, and
Kazuo Kurokawa, and
Pranoy Sahu, and
Bernadette Lombardi, and
Domenico Supino, and
Mikhail A Zhukovsky, and
Anthony Vocat, and
Prathyush Pothukuchi, and
Vidya Kunnathully, and
Laura Capolupo, and
Gaelle Boncompain, and
Carlo Vitagliano, and
Federica Zito Marino, and
Gabriella Aquino, and
Daniela Montariello, and
Petra Henklein, and
Luigi Mandrich, and
Gerardo Botti, and
Henrik Clausen, and
Ulla Mandel, and
Toshiyuki Yamaji, and
Kentaro Hanada, and
Alfredo Budillon, and
Franck Perez, and
Seetharaman Parashuraman, and
Yusuf A Hannun, and
Akihiko Nakano, and
Daniela Corda, and
Giovanni D'Angelo, and
Alberto Luini
Institute of Biochemistry and Cell Biology, National Research Council, Naples, Italy.
Glycosphingolipids are important components of the plasma membrane where they modulate the activities of membrane proteins including signalling receptors. Glycosphingolipid synthesis relies on competing reactions catalysed by Golgi-resident enzymes during the passage of substrates through the Golgi cisternae. The glycosphingolipid metabolic output is determined by the position and levels of the enzymes within the Golgi stack, but the mechanisms that coordinate the intra-Golgi localisation of the enzymes are poorly understood. Here, we show that a group of sequentially-acting enzymes operating at the branchpoint among glycosphingolipid synthetic pathways binds the Golgi-localised oncoprotein GOLPH3. GOLPH3 sorts these enzymes into vesicles for intra-Golgi retro-transport, acting as a component of the cisternal maturation mechanism. Through these effects, GOLPH3 controls the sub-Golgi localisation and the lysosomal degradation rate of specific enzymes. Increased GOLPH3 levels, as those observed in tumours, alter glycosphingolipid synthesis and plasma membrane composition thereby promoting mitogenic signalling and cell proliferation. These data have medical implications as they outline a novel oncogenic mechanism of action for GOLPH3 based on glycosphingolipid metabolism.
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