Leptin in the rat's nucleus accumbens (NAcc) core has previously shown to disrupt the effects of acute administration of cocaine on both locomotor activity and the phosphorylation levels of glycogen synthase kinase 3β. In the present study, we further measured the phosphorylation levels of GluA1 after bilateral microinjections of leptin in this site followed by acute administration of cocaine. Interestingly, leptin in the NAcc core significantly blocks the increase of GluA1 phosphorylation levels at serine 845 induced by acute administration of cocaine. These effects were not observed for GluA1 phosphorylation levels at serine 831. We have also found additional evidence that glycogen synthase kinase 3β may play a major role in mediating these processes.
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http://dx.doi.org/10.1097/WNR.0000000000001001 | DOI Listing |
Mol Biol Rep
January 2025
Department of Molecular Biology Vadi Kampüsü, Istanbul Atlas University, Anadolu Cd., No 40, Kağıthane, Istanbul, 34408, Turkey.
Background: Modulation of protein synthesis according to the physiological cues is maintained through tight control of Eukaryotic Elongation Factor 2 (eEF2), whose unique translocase activity is essential for cell viability. Phosphorylation of eEF2 at its Thr56 residue inactivates this function in translation. In our previous study we reported a novel mode of post-translational modification that promotes higher efficiency in T56 phosphorylation.
View Article and Find Full Text PDFChem Biodivers
January 2025
Biruni Universitesi, Molecular Biology and Genetics, Biruni Uni, İstanbul, TURKEY.
Regulation of protein production in response to physiological signals is achieved through precise control of Eukaryotic Elongation Factor 2 (eEF2), whose distinct translocase function is crucial for cell survival. Phosphorylation of eEF2 at its Thr56 (T56) residue inactivates this function in translation. Using genetically modified paralogue of a colon cancer cell line, HCT116 which carries a point mutation at Ser595-to-Alanine in the eEF2 gene we were able to create a constitutively active form of eEF2.
View Article and Find Full Text PDFAm J Cancer Res
December 2024
Department of Pharmacology and Toxicology, Medical College of Wisconsin Milwaukee, Wisconsin 53226, USA.
Cancer cell overexpresses numerus proteins, however, how these up-regulated proteins, especially those enzymatically opposite kinases and phosphatases, act together to promote oncogenesis is unknown. Here, we reported that protein tyrosine phosphatase H1 (PTPH1) is a scaffold protein for receptor tyrosine kinase (HER2) to potentiate breast tumorigenesis. PTPH1 utilizes its PDZ domain to bind HER2, p38γ, PBK, and YAP1 and to increase HER2 nuclear translocation, stemness, and oncogenesis.
View Article and Find Full Text PDFJ Mol Cell Cardiol Plus
September 2024
O'Brien Institute Department, St Vincent's Institute of Medical Research, Victoria 3065, Australia.
Dynamin-related protein 1 (Drp1) is a mitochondrial fission protein and a viable target for cardioprotection against myocardial ischaemia-reperfusion injury. Here, we reported a novel Drp1 inhibitor (DRP1i1), delivered using a cardiac-targeted nanoparticle drug delivery system, as a more effective approach for achieving acute cardioprotection. DRP1i1 was encapsulated in cubosome nanoparticles with conjugated cardiac-homing peptides (NanoDRP1i1) and the encapsulation efficiency was 99.
View Article and Find Full Text PDFUnlabelled: SHP1 (PTPN6) and SHP2 (PTPN11) are closely related protein-tyrosine phosphatases (PTPs), which are autoinhibited until their SH2 domains bind paired tyrosine-phosphorylated immunoreceptor tyrosine-based inhibitory/switch motifs (ITIMs/ITSMs). These PTPs bind overlapping sets of ITIM/ITSM-bearing proteins, suggesting that they might have some redundant functions. By studying T cell-specific single and double knockout mice, we found that SHP1 and SHP2 redundantly restrain naïve T cell differentiation to effector and central memory phenotypes, with SHP1 playing the dominant role.
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