Tripartite motif-containing protein (TRIM) family proteins are involved in a broad range of biological processes and, consistently, their alterations result in diverse pathological conditions such as genetic diseases, viral infection and cancer development. In this study, we found that one of the TRIM family proteins, TRIM31, is highly expressed in the gastrointestinal tract and interacts with p52(Shc), one of the signal transducers. We also found by a binding assay that almost the whole region other than the RING domain is required for the binding to p52(Shc) but found by pulse-chase analysis that overexpression of TRIM31 does not affect the stability of p52(Shc). Moreover, we found that overexpression of TRIM31 suppresses anchorage-independent cell growth induced by the active form of c-Src. These results suggest that TRIM31 attenuates c-Src signaling via p52(Shc) under anchorage-independent growth conditions and is potentially associated with growth activity of cells in the gastrointestinal tract.
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http://dx.doi.org/10.1016/j.bbrc.2009.08.028 | DOI Listing |
Int J Mol Sci
November 2024
Laboratory of Mitochondrial Biology and Metabolism, Nencki Institute of Experimental Biology of Polish Academy of Sciences, 02-093 Warsaw, Poland.
Biomed Pharmacother
December 2020
Department of Molecular Biosciences, 1089 Veterinary Medicine Dr., VM3B, UC Davis, CA, 95616, USA. Electronic address:
There has been little innovation in identifying novel insulin sensitizers. Metformin, developed in the 1920s, is still used first for most Type 2 diabetes patients. Mice with genetic reduction of p52Shc protein have improved insulin sensitivity and glucose tolerance.
View Article and Find Full Text PDFAgeing Res Rev
November 2020
Department of Biotechnology, University of Kashmir, Srinagar, Jammu and Kashmir, 190006, India. Electronic address:
ShcA (Src homologous- collagen homologue), family of adapter proteins, consists of three isoforms which integrate and transduce external stimuli to different signaling networks. ShcA family consists of p46Shc, p52Shc and p66Shc isoforms, characterized by having multiple protein-lipid and protein-protein interaction domains implying their functional diversity. Among the three isoforms p66Shc is structurally different containing an additional CH2 domain which attributes to its dual functionality in cell growth, mediating both cell proliferation and apoptosis.
View Article and Find Full Text PDFHepatology
October 2020
Gastroenterology and Hepatology, Stanford University, Stanford, CA.
Background And Aims: Older patients with obesity/type II diabetes mellitus frequently present with advanced NASH. Whether this is due to specific molecular pathways that accelerate fibrosis during aging is unknown. Activation of the Src homology 2 domain-containing collagen-related (Shc) proteins and redox stress have been recognized in aging; however, their link to NASH has not been explored.
View Article and Find Full Text PDFPharmacol Res
November 2018
Department of Molecular Biosciences, 1089 Veterinary Medicine Dr., VM3B, UC Davis, CA, 95616, USA. Electronic address:
When insulin binds insulin receptor, IRS1 signaling is stimulated to trigger the maximal insulin response. p52Shc protein competes directly with IRS1, thus damping and diverting maximal insulin response. Genetic reduction of p52Shc minimizes competition with IRS1, and improves insulin signaling and glucose control in mice, and improves pathophysiological consequences of hyperglycemia.
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