ArticleMolecular and cellular biology2013
DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with the plasma membrane.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024Review
- DHHC17 Is a New Regulator of AMPK Signaling.Molecular and cellular biology · 2022Article
- Substrate recruitment by zDHHC protein acyltransferases.Open biology · 2021Article
- Regulatory effects of protein S-acylation on insulin secretion and insulin action.Open biology · 2021Review
- Putative Role of Protein Palmitoylation in Cardiac Lipid-Induced Insulin Resistance.International journal of molecular sciences · 2020Review
- Regulatory effects of post-translational modifications on zDHHCThe Journal of biological chemistry · 2020Review
- Acylation - A New Means to Control Traffic Through the Golgi.Frontiers in cell and developmental biology · 2019Review
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- DNA-Methylation and Body Composition in Preschool Children: Epigenome-Wide-Analysis in the European Childhood Obesity Project (CHOP)-Study.Scientific reports · 2017Article
- Peptide array-based screening reveals a large number of proteins interacting with the ankyrin-repeat domain of the zDHHC17The Journal of biological chemistry · 2017Article
- Protein palmitoylation: Palmitoyltransferases and their specificity.Experimental biology and medicine (Maywood, N.J.) · 2017Article
- DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4 Membrane Translocation.The Journal of biological chemistry · 2017Article
- The canonical DHHC motif is not absolutely required for the activity of the yeast S-acyltransferases Swf1 and Pfa4.The Journal of biological chemistry · 2015Article
- Identification of a Novel Sequence Motif Recognized by the Ankyrin Repeat Domain of zDHHC17/13 S-Acyltransferases.The Journal of biological chemistry · 2015Article
- Curation of the Mammalian Palmitoylome Indicates a Pivotal Role for Palmitoylation in Diseases and Disorders of the Nervous System and Cancers.PLoS computational biology · 2015Article
- Glut4 palmitoylation at Cys223 plays a critical role in Glut4 membrane trafficking.Biochemical and biophysical research communications · 2015Article
- The physiology of protein S-acylation.Physiological reviews · 2015Review
- ClipR-59 interacts with Elmo2 and modulates myoblast fusion.The Journal of biological chemistry · 2015Article
- The Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activity.Molecular biology of the cell · 2014Article
- The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease.Human molecular genetics · 2014Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
ClipR-59 interacts with Akt and regulates Akt compartmentalization and Glut4 membrane trafficking in a plasma membrane association-dependent manner. The association of ClipR-59 with plasma membrane is mediated by ClipR-59 palmitoylation at Cys534 and Cys535. To understand the regulation of ClipR-59 palmitoylation, we have examined all known mammalian DHHC palmitoyltransferases with respect to their ability to promote ClipR-59 palmitoylation. We found that, among 23 mammalian DHHC palmitoyltransferases, DHHC17 is the major ClipR-59 palmitoyltransferase, as evidenced by the fact that DHHC17 interacted with ClipR-59 and palmitoylated ClipR-59 at Cys534 and Cys535. By palmitoylating ClipR-59, DHHC17 directly regulates ClipR-59 plasma membrane association, as ectopic expression of DHHC17 increased whereas silencing of DHHC17 reduced the levels of ClipR-59 associated with plasma membrane. We have also examined the role of DHHC17 in Akt signaling and found that silencing of DHHC17 in 3T3-L1 adipocytes decreased the levels of Akt as well as ClipR-59 on the plasma membrane and impaired insulin-dependent Glut4 membrane translocation. We suggest that DHHC17 is a ClipR-59 palmitoyltransferase that modulates ClipR-59 plasma membrane binding, thereby regulating Akt signaling and Glut4 membrane translocation in adipocytes.
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