ArticleMolecular and cellular biology2009
ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Palmitoylation: an emerging therapeutic target bridging physiology and disease.Cellular & molecular biology letters · 2025Review
- Cell cycle gene regulation dynamics revealed by RNA velocity and deep-learning.Nature communications · 2022Article
- Article
- AKT ISOFORMS-AS160-GLUT4: The defining axis of insulin resistance.Reviews in endocrine & metabolic disorders · 2021Review
- Role of Akt isoforms in neuronal insulin signaling and resistance.Cellular and molecular life sciences : CMLS · 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
- Akt-ing Up Just About Everywhere: Compartment-Specific Akt Activation and Function in Receptor Tyrosine Kinase Signaling.Frontiers in cell and developmental biology · 2019Review
- DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4 Membrane Translocation.The Journal of biological chemistry · 2017Article
- Elmo2 Is a Regulator of Insulin-dependent Glut4 Membrane Translocation.The Journal of biological chemistry · 2016Article
- Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response.The Biochemical journal · 2015Article
- ClipR-59 interacts with Elmo2 and modulates myoblast fusion.The Journal of biological chemistry · 2015Article
- DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with the plasma membrane.Molecular and cellular biology · 2013Article
- Greater insulin-mediated Akt phosphorylation concomitant with heterogeneous effects on phosphorylation of Akt substrates in soleus of calorie-restricted rats.American journal of physiology. Regulatory, integrative and comparative physiology · 2012Article
- Changes in CLIP3 expression after sciatic nerve injury in adult rats.Journal of molecular histology · 2012Article
- The association of ClipR-59 protein with AS160 modulates AS160 protein phosphorylation and adipocyte Glut4 protein membrane translocation.The Journal of biological chemistry · 2012Article
- CLIPR-59 regulates TNF-α-induced apoptosis by controlling ubiquitination of RIP1.Cell death & disease · 2012Article
- Gastric inhibitory peptide controls adipose insulin sensitivity via activation of cAMP-response element-binding protein and p110β isoform of phosphatidylinositol 3-kinase.The Journal of biological chemistry · 2011Article
- Differential muscle gene expression as a function of disease progression in Goto-Kakizaki diabetic rats.Molecular and cellular endocrinology · 2011Article
- Regulation of adipocyte differentiation by distinct subcellular pools of protein kinase B (PKB/Akt).The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Akt is activated on the plasma membrane and its substrates are distributed throughout various cellular compartments. To phosphorylate its substrates, Akt needs to be recruited to specific intracellular compartments. Thus, regulation of Akt cellular compartmentalization constitutes an important mechanism to specify Akt signaling. Here, we report the identification of ClipR-59 as an Akt interaction protein. We show that the interaction of ClipR-59 with Akt is mediated by the CAP-Gly domain of ClipR-59 and kinase domain of Akt and is regulated by Akt phosphorylation. We demonstrate that ClipR-59 regulates the Akt membrane association through its interaction with Akt and membrane localization and, by modulating Akt cellular compartmentalization, differentially modulates phosphorylation of Akt substrates in adipocytes. Finally, we provide evidence that one of the Akt substrates whose phosphorylation is upregulated by ClipR-59 is AS160, a negative regulator of adipocyte glucose transport. Accordingly, ectopic expression of ClipR-59 enhances, whereas knockdown of ClipR-59 suppresses, adipocyte glucose transport. We suggest that ClipR-59 functions as a scaffold protein that interacts with phospho-Akt and recruits active Akt on the membrane and may play an important role in adipocyte glucose transport.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.