PKD-dependent PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 is required for E-cadherin transport from Golgi to plasma membrane.

Autor:	Grimaldi G; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Filograna A; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Schembri L; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Lo Monte M; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Di Martino R; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Pirozzi M; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Spano D; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Beccari AR; Drug Discovery Platform, Dompé Farmaceutici SpA Research Center, 67100 L'Aquila, Italy., Parashuraman S; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Luini A; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Valente C; Institute for Endocrinology and Experimental Oncology 'G. Salvatore,' National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.; Institute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy., Corda D; Department of Biomedical Sciences, National Research Council, 00185 Rome, Italy g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Jan 04; Vol. 119 (1).
DOI:	10.1073/pnas.2026494119
Abstrakt:	Adenosine diphosphate (ADP)-ribosylation is a posttranslational modification involved in key regulatory events catalyzed by ADP-ribosyltransferases (ARTs). Substrate identification and localization of the mono-ADP-ribosyltransferase PARP12 at the trans -Golgi network (TGN) hinted at the involvement of ARTs in intracellular traffic. We find that Golgin-97, a TGN protein required for the formation and transport of a specific class of basolateral cargoes (e.g., E-cadherin and vesicular stomatitis virus G protein [VSVG]), is a PARP12 substrate. PARP12 targets an acidic cluster in the Golgin-97 coiled-coil domain essential for function. Its mutation or PARP12 depletion, delays E-cadherin and VSVG export and leads to a defect in carrier fission, hence in transport, with consequent accumulation of cargoes in a trans -Golgi/Rab11-positive intermediate compartment. In contrast, PARP12 does not control the Golgin-245-dependent traffic of cargoes such as tumor necrosis factor alpha (TNFα). Thus, the transport of different basolateral proteins to the plasma membrane is differentially regulated by Golgin-97 mono-ADP-ribosylation by PARP12. This identifies a selective regulatory mechanism acting on the transport of Golgin-97- vs. Golgin-245-dependent cargoes. Of note, PARP12 enzymatic activity, and consequently Golgin-97 mono-ADP-ribosylation, depends on the activation of protein kinase D (PKD) at the TGN during traffic. PARP12 is directly phosphorylated by PKD, and this is essential to stimulate PARP12 catalytic activity. PARP12 is therefore a component of the PKD-driven regulatory cascade that selectively controls a major branch of the basolateral transport pathway. We propose that through this mechanism, PARP12 contributes to the maintenance of E-cadherin-mediated cell polarity and cell-cell junctions. Competing Interests: The authors declare no competing interest. (Copyright © 2021 the Author(s). Published by PNAS.)
Databáze:	MEDLINE
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