Limited redundancy of survival signals from the type 1 insulin-like growth factor receptor.

Abstract	The type 1 insulin-like growth factor receptor (IGF-IR) is effective in protecting cells from a variety of apoptotic injuries. In 32D murine hemopoietic cells, the IGF-IR sends three separate survival signals, through insulin receptor substrate-1, Shc, and mitochondrial Raf translocation. We report here that these three pathways for survival have a limited redundancy. If one of these pathways is blocked, the IGF-IR can still protect 32D cells from apoptosis induced by interleukin-3 withdrawal. However, when two of the three pathways are inactivated, the receptor is no longer capable to protect cells from apoptosis. The survival signal can use any two pathway combinations.
Authors	M Navarro, R Baserga
Journal	Endocrinology (Endocrinology) Vol. 142 Issue 3 Pg. 1073-81 (Mar 2001) ISSN: 0013-7227 [Print] United States
PMID	11181521 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References	Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Chromones Enzyme Inhibitors Flavonoids Insulin Receptor Substrate Proteins Irs1 protein, mouse Morpholines Phosphoproteins Proteins Proto-Oncogene Proteins Shc Signaling Adaptor Proteins Shc1 protein, mouse Src Homology 2 Domain-Containing, Transforming Protein 1 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one Receptor, IGF Type 1 Protein Serine-Threonine Kinases Proto-Oncogene Proteins c-akt Proto-Oncogene Proteins c-raf Mitogen-Activated Protein Kinases 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one
Topics	Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Animals Apoptosis (drug effects) Cell Line Cell Survival (physiology) Chromones (pharmacology) Enzyme Activation (physiology) Enzyme Inhibitors (pharmacology) Flavonoids (pharmacology) Hematopoietic Stem Cells (physiology) Insulin Receptor Substrate Proteins Mice Mitogen-Activated Protein Kinases (metabolism) Morpholines (pharmacology) Phosphoproteins (metabolism) Phosphorylation Protein Serine-Threonine Kinases Proteins (metabolism) Proto-Oncogene Proteins (metabolism) Proto-Oncogene Proteins c-akt Proto-Oncogene Proteins c-raf (pharmacology) Receptor, IGF Type 1 (physiology) Shc Signaling Adaptor Proteins Signal Transduction (drug effects, physiology) Src Homology 2 Domain-Containing, Transforming Protein 1

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