Results: 4

1.
Figure  1

Figure 1. From: Protean PTEN: Form and Function.

Germline PTEN mutations in CS, BRRS, PS, and Proteus-like syndromes

Kristin A. Waite, et al. Am J Hum Genet. 2002 April;70(4):829-844.
2.
Figure  3

Figure 3. From: Protean PTEN: Form and Function.

PTEN as a regulator of the PI3K pathway. Ligand binding to membrane receptors results in the activation of PI3K and the subsequent increase in PIP3, which recruits PDK1 to the cellular membrane. PDK1 phosphorylates and activates AKT, which in turn regulates a variety of cellular processes. PTEN dephosphorylates PI3P, lowering its cellular levels and resulting in the down-regulation of AKT.

Kristin A. Waite, et al. Am J Hum Genet. 2002 April;70(4):829-844.
3.
Figure  4

Figure 4. From: Protean PTEN: Form and Function.

PTEN as a modulator of the MAPK pathway. PTEN can inhibit the activation of MAPK by several mechanisms. By dephosphorylating Shc and/or IRS-1, PTEN prevents the association of these proteins to the Sos:Grb complex, which is required for MAPK activation. Gab interacts with the membrane by binding to PI3P regions via the pleckstrin-homology domain. By decreasing the PI3P levels in the membrane, PTEN inhibits the translocation of Gab to the membrane and its subsequent activation of the MAPK pathways. The entire pathway for MAPK activation and protein-protein interactions has been omitted for clarity.

Kristin A. Waite, et al. Am J Hum Genet. 2002 April;70(4):829-844.
4.
Figure  2

Figure 2. From: Protean PTEN: Form and Function.

Protein domains of PTEN. The N-terminal phosphatase domain (amino acids 1–185) is shown with the catalytic core. The missense mutations which have been crucial for the elucidation of the cellular role of PTEN are highlighted in orange. Mutations at C124 render a lipid- and protein-phosphatase–inactive protein, whereas mutations at G129 result in a lipid-phosphatase–inactive yet protein-phosphatase–active PTEN. The C-terminal domain (amino acids 186–403) contains the lipid-binding C2 domain (amino acids 186–351); PEST domains (amino acids 350–375 and 379–396), which regulate protein stability; and the PDZ domain, which is important in protein-protein interactions. The CK2 phosphorylation sites (S380, T382, and T383), which are important for stability, are indicated by the blue asterisks (*).

Kristin A. Waite, et al. Am J Hum Genet. 2002 April;70(4):829-844.

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