Phosphorylation of AKT: a Mutational Analysis.

Jonathan R. Hart; Peter K. Vogt

doi:10.18632/oncotarget.293

Oncotarget

Oncotarget (a primarily oncology-focused, peer-reviewed, open access journal) aims to maximize research impact through insightful peer-review; eliminate borders between specialties by linking different fields of oncology, cancer research and biomedical sciences; and foster application of basic and clinical science.

Its scope is unique. The term "oncotarget" encompasses all molecules, pathways, cellular functions, cell types, and even tissues that can be viewed as targets relevant to cancer as well as other diseases. The term was introduced in the inaugural Editorial, Introducing Oncotarget.

As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. Papers will now be published continuously within yearly volumes in their final and complete form and then quickly released to Pubmed.

Subscribe to receive alerts once a paper has been published by Oncotarget.

Impact Journals, LLC is the publisher of Oncotarget: www.impactjournals.com.

Impact Journals is a member of the Wellcome Trust List of Compliant Publishers.

Impact Journals is a member of the Society for Scholarly Publishing.

On December 23, 2022, Oncotarget server experienced a DDoS attack. As a result, Oncotarget site was inaccessible for a few hours. Oncotarget team swiftly dealt with the situation and took it under control. This malicious action will be reported to the FBI.

Research Papers:

Phosphorylation of AKT: a Mutational Analysis.

Jonathan R. Hart _ and Peter K. Vogt

PDF | HTML | Supplementary Files | How to cite

Oncotarget. 2011; 2:467-476. https://doi.org/10.18632/oncotarget.293

Metrics: PDF 4848 views | HTML 6305 views | ?

Abstract

Jonathan R. Hart, Peter K. Vogt

¹The Scripps Research Institute, Molecular and Experimental Medicine, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

Keywords: Oncogenic transformation, signaling, myristylation, phosphomimetic

Received: June 9, 2011; Accepted: June 10, 2011; Published: June 10, 2011;

Correspondence:

Jonathan R. Hart, e-mail:

Abstract

Akt (cellular homolog of murine thymoma virus akt8 oncogene) is an essential component of the PI3K (phosphatidylinositol 3-kinase) pathway. Its activity is stimulated by receptor tyrosine kinases and G-protein coupled receptors and plays a critical role in the regulation of cell proliferation, differentiation and apoptosis. A gain of function in Akt can lead to uncontrolled cell proliferation and resistance to apoptosis, both hallmarks of oncogenic transformation. In this communication, we have investigated the phosphorylation at the Akt residues T308, S473 and T450 and their roles in oncogenic transformation and signaling. We find that T450 phosphorylation has only a minimal part in these activities. In contrast, the phosphorylation of T308 and of S473 fulfills essential, distinct, and non-overlapping functions that we define with inactivating and with phosphomimetic mutations of these sites.

All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 4.0 License.
PII: 293

Publication Alerts

Research Papers:

Phosphorylation of AKT: a Mutational Analysis.

Abstract