AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation
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Summary
Evidence is presented that the AH/PH domain is a domain of protein-protein interaction which mediates the formation of Akt protein complexes and the interaction between c-akt AH/ PH domains is highly specific, as determined by the failure of this domain to bind AKT2.
- Type
- article
- Published
- 1995-04-01
- Cited by
- 178
- References
- 30
- Access
- Open access
- OpenAlex
- https://openalex.org/W1858533191
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25151772
Keywords
Biology, Protein kinase B, Proto-Oncogene Proteins c-akt, Domain (mathematical analysis), Cell biology
References
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Cited by
- Targets of B‐cell antigen receptor signaling: the phosphatidylinositol 3‐kinase/Akt/glycogen synthase kinase‐3 signaling pathway and the Rap1 GTPase
- BSTA Promotes mTORC2-Mediated Phosphorylation of Akt1 to Suppress Expression of FoxC2 and Stimulate Adipocyte Differentiation
- Modulation Insulin-responsiver Signalwege durch Flavonoide
- Systems biology analyses of hematopoietic cells
- Aktivierung des Akt/FoxO-Signalweges durch Insulin und Schwermetallionen: transkriptionelle Regulation der Biosynthese von Selenoprotein P
- Cell-cycle control by protein kinase B
- PTEN suppresses breast cancer cell growth by phosphatase activity-dependent G1 arrest followed by cell death.
- Targeting the translational apparatus to improve leukemia therapy: roles of the PI3K/PTEN/Akt/mTOR pathway
- Glial cell line‐derived neurotrophic factor receptor‐alpha 1 expressed in striatum in trans regulates development and injury response of dopamine neurons of the substantia nigra
- PKB phosphorylation and survivin expression are cooperatively regulated by disruption of microfilament cytoskeleton
- B cell antigen receptor signaling 101.
- Mechanism of Protein Kinase B Activation by Cyclic AMP-Dependent Protein Kinase
- The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells.
- Akt/PKB localisation and 3' phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction.
- The role of the PH domain in the signal‐dependent membrane targeting of Sos
- Regulation of the Akt kinase by interacting proteins
- A phosphoinositide‐binding sequence is shared by PH domain target molecules—a model for the binding of PH domains to proteins
- Differential Regulation of Akt Kinase Isoforms by the Members of the TCL1 Oncogene Family*
- Expression of mRNA for Akt, serine-threonine protein kinase, in the brain during development and its transient enhancement following axotomy of hypoglossal nerve
- Akt Forms an Intracellular Complex with Heat Shock Protein 90 (Hsp90) and Cdc37 and Is Destabilized by Inhibitors of Hsp90 Function*
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