J Korean Soc Endocrinol.  2005 Oct;20(5):434-440. 10.3803/jkes.2005.20.5.434.

Regulation of Insulin Signaling through Protein Degradation

• Lee MY
• Baek KH

• KMID: 2200589
• DOI: http://doi.org/10.3803/jkes.2005.20.5.434

Abstract

No abstract available.

MeSH Terms

Insulin*
Proteolysis*
Insulin

Figure

• 

  Fig. 1 Ubiquitin-proteasome pathway. Ubiquitination requires a series of enzymes, which include ubiquitin activating enzymes (E1), ubiquitin conjugating enzymes (E2), ubiquitin ligases (E3), and ubiquitin factor (E4) which are essential for efficient polyubiquitination. Ubiquitinated proteins are recognized and degraded by 26S proteasome through the process known as ubiquitin-mediated proteolysis in an ATP dependent manner.

• 

  Fig. 2 Insulin signaling pathway. Binding of insulin to its receptors induces autophosphorylation at a number of tyrosine residues. The insulin receptor then phosphorylates IRS molecules at numerous tyrosine residues, some of which are recognized by the Src homology 2 (SH2) domain of the p85 regulatory subunit of a lipid kinase, PI3-kinase. The catalytic subunit of PI3-kinase then phosphorylates PtdIns(4,5)P2 at the plasma membrane of cells to generate the second messenger Ptdlns(3,4,5)P3 (PIP3) which stimulates insulin-dependent processes. BAD, BCL2 antagonist of cell death; CAP, c-Cbl-associated protein; CBL, CAS-BR-M murine ecotropic retroviral transforming sequence homolog; FOXO, Forkhead transcription factor; GSK3, GS kinase; PIP, phosphatidylinositol polyphosphate; PK, protein kinase; PPAR, peroxisome proliferator-activated receptor; SREBP, sterol regulatory element-binding protein.

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