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  Distinct signaling by insulin and IGF-1 receptors and their extra- and intracellular domains

Nagao, H., Cai, W., Wewer Albrechtsen, N. J., Steger, M., Batista, T. M., Pan, H., et al. (2021). Distinct signaling by insulin and IGF-1 receptors and their extra- and intracellular domains. Proceedings of the National Academy of Sciences of the United States of America, 118(17): e2019474118. doi:10.1073/pnas.2019474118.

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 Creators:
Nagao, Hirofumi1, Author
Cai, Weikang1, Author
Wewer Albrechtsen, Nicolai J.2, Author              
Steger, Martin2, Author              
Batista, Thiago M.1, Author
Pan, Hui1, Author
Dreyfuss, Jonathan M.1, Author
Mann, Matthias2, Author              
Kahn, C. Ronald1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: GROWTH-FACTOR RECEPTOR; PROTEINS; KINASE; DEATH; REQUIREMENT; VIMENTINScience & Technology - Other Topics; insulin signaling; protein phosphorylation; cellular signaling; IGF-1 signaling; kinases;
 Abstract: Insulin and insulin-like growth factor 1 (IGF-1) receptors share many downstream signaling pathways but have unique biological effects. To define the molecular signals contributing to these distinct activities, we performed global phosphoproteomics on cells expressing either insulin receptor (IR), IGF-1 receptor (IGF1R), or chimeric IR-IGF1R receptors. We show that IR preferentially stimulates phosphorylations associated with mammalian target of rapamycin complex 1 (mTORC1) and Akt pathways, whereas IGF1R preferentially stimulates phosphorylations on proteins associated with the Ras homolog family of guanosine triphosphate hydrolases (Rho GTPases), and cell cycle progression. There were also major differences in the phosphoproteome between cells expressing IR versus IGF1R in the unstimulated state, including phosphorylation of proteins involved in membrane trafficking, chromatin remodeling, and cell cycle. In cells expressing chimeric IR-IGF1R receptors, these differences in signaling could be mapped to contributions of both the extra- and intracellular domains of these receptors. Thus, despite their high homology, IR and IGF1R preferentially regulate distinct networks of phosphorylation in both the basal and stimulated states, allowing for the unique effects of these hormones on organismal function.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published online
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000647796500013
DOI: 10.1073/pnas.2019474118
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 118 (17) Sequence Number: e2019474118 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230