Adiponectin receptor 1 C-terminus interacts with PDZ-domain proteins such as syntrophins
| Autor: | E. Eggenhofer, Sandra Schmidhofer, Christa Buechler, Yvonne Hader, Markus Neumeier, Marvin E. Adams, Sabrina Krautbauer, Stanley C. Froehner, Wolfgang Mages, Kristina Eisinger |
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| Rok vydání: | 2013 |
| Předmět: |
Male
Two-hybrid screening Immunoblotting Clinical Biochemistry PDZ domain Fluorescent Antibody Technique PDZ Domains Peptide Biology Transfection p38 Mitogen-Activated Protein Kinases Article Cell Line Pathology and Forensic Medicine Mice AMP-Activated Protein Kinase Kinases Two-Hybrid System Techniques Animals Humans Receptor Molecular Biology Syntrophin Mice Knockout chemistry.chemical_classification Adiponectin receptor 1 C-terminus Enzyme Activation Mice Inbred C57BL chemistry Biochemistry Dystrophin-Associated Proteins Hepatocytes Phosphorylation Receptors Adiponectin Protein Kinases |
| Zdroj: | Experimental and Molecular Pathology. 95:180-186 |
| ISSN: | 0014-4800 |
| DOI: | 10.1016/j.yexmp.2013.07.002 |
| Popis: | Adiponectin receptor 1 (AdipoR1) is one of the two signaling receptors of adiponectin with multiple beneficial effects in metabolic diseases. AdipoR1 C-terminal peptide is concordant with the consensus sequence of class I PSD-95, disc large, ZO-1 (PDZ) proteins, and screening of a liver yeast two hybrid library identified binding to β2-syntrophin (SNTB2). Hybridization of a PDZ-domain array with AdipoR1 C-terminal peptide shows association with PDZ-domains of further proteins including β1- and α-syntrophin (SNTA). Interaction of PDZ proteins and C-terminal peptides requires a free carboxy terminus next to the PDZ-binding region and is blocked by carboxy terminal added tags. N-terminal tagged AdipoR1 is more highly expressed than C-terminal tagged receptor suggesting that the free carboxy terminus may form a complex with PDZ proteins to regulate cellular AdipoR1 levels. The C- and N-terminal tagged AdipoR1 proteins are mainly localized in the cytoplasma. N-terminal but not C-terminal tagged AdipoR1 colocalizes with syntrophins in adiponectin incubated Huh7 cells. Adiponectin induced hepatic phosphorylation of AMPK and p38 MAPK which are targets of AdipoR1 is, however, not blocked in SNTA and SNTB2 deficient mice. Further, AdipoR1 protein is similarly abundant in the liver of knock-out and wild type mice when kept on a standard chow or a high fat diet. In summary these data suggest that AdipoR1 protein levels are regulated by so far uncharacterized class I PDZ proteins which are distinct from SNTA and SNTB2. |
| Databáze: | OpenAIRE |
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