Faculty Opinions recommendation of Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.

2002 ◽  
Author(s):  
Patricia Jennings
Keyword(s):  
Protein Kinase ◽  
Molecular Mechanism ◽  
Protein Kinase B ◽  
Hydrophobic Motif

scholarly journals Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation

2002 ◽  
Vol 9 (6) ◽  
pp. 1227-1240 ◽  
Author(s):  
Jing Yang ◽  
Peter Cron ◽  
Vivienne Thompson ◽  
Valerie M. Good ◽  
Daniel Hess ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Molecular Mechanism ◽  
Protein Kinase B ◽  
Hydrophobic Motif

Molecular Mechanism of Extractum Liquidum Drug Loading Materials on Promoting Chronic Wound Tissue Repair Through Phosphatidylinositol 3 Kinase/Protein Kinase B/Hypoxia Induction Factor 1α Signal Pathway

2022 ◽  
Vol 12 (1) ◽  
pp. 52-60
Author(s):  
Hui Ji ◽  
Qian Zhang ◽  
Zengmin Yang ◽  
Minjie Rui ◽  
Qiyi Chen ◽  
...  
Keyword(s):  
Wound Healing ◽  
Protein Kinase ◽  
Molecular Mechanism ◽  
Healing Rate ◽  
Chronic Wound ◽  
Protein Kinase B ◽  
Signal Molecules ◽  
Group Model ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphatidylinositol 3

To solve the shortcomings of traditional Zeji extractum liquidum (traditional Chinese medicine used for wound healing), and to explore the effect of Zeji Etractum Lquidum (ZLE) Nano Materials (ZLENM) on chronic wound (CW) healing and its molecular mechanism. 30 SD rats were divided into 3 groups in random: control group (Ctrl group), model group (CW group), and treatment group (ZLENM group). The results of wound healing rate showed that, in contrast with the CW, the healing rate of back wounds in the ZLENM group was greatly increased on the 7th and 14th days (P < 0.05). In contrast with the Ctrl, the rats in the CW and the ZLENM groups had greatly increased CD31 positive staining on the 7th and 14th days (P < 0.05), and the CW was lower than the ZLENM group (P < 0.05). In contrast with the 7th day, the MVD in the CW and the ZLENM groups was greatly reduced on the 14th day (P < 0.05). Western blot analysis of the expression of related signal molecules showed that the expressions of P-Akt, P-PI3K, HIF-1α, and VEGFR2 protein in the wounds in the CW and ZLENM groups were greatly increased in contrast with the Ctrl (P < 0.05), and CW was lower than ZLENM group (P < 0.05). In conclusion, ZLENM can promote wound healing and increase the number of wound angiogenesis in CW rats. The mechanism is related to the activation of phosphatidylinositol 3 kinase/protein kinase B/hypoxia induction factor 1α (PI3K/AKT/HIF-1α) signaling pathway.

scholarly journals Identification of Protor as a novel Rictor-binding component of mTOR complex-2

2007 ◽  
Vol 405 (3) ◽  
pp. 513-522 ◽  
Author(s):  
Laura R. Pearce ◽  
Xu Huang ◽  
Jérôme Boudeau ◽  
Rafał Pawłowski ◽  
Stephan Wullschleger ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase B ◽  
Mammalian Target Of Rapamycin ◽  
Specific Component ◽  
S6 Kinase ◽  
Important Regulator ◽  
Hydrophobic Motif ◽  
Triton X ◽  
Binding Subunit ◽  
Binding Component

The mTOR (mammalian target of rapamycin) protein kinase is an important regulator of cell growth. Two complexes of mTOR have been identified: complex 1, consisting of mTOR–Raptor (regulatory associated protein of mTOR)–mLST8 (termed mTORC1), and complex 2, comprising mTOR–Rictor (rapamycininsensitive companion of mTOR)–mLST8–Sin1 (termed mTORC2). mTORC1 phosphorylates the p70 ribosomal S6K (S6 kinase) at its hydrophobic motif (Thr389), whereas mTORC2 phosphorylates PKB (protein kinase B) at its hydrophobic motif (Ser473). In the present study, we report that widely expressed isoforms of unstudied proteins termed Protor-1 (protein observed with Rictor-1) and Protor-2 interact with Rictor and are components of mTORC2. We demonstrate that immunoprecipitation of Protor-1 or Protor-2 results in the co-immunoprecipitation of other mTORC2 subunits, but not Raptor, a specific component of mTORC1. We show that detergents such as Triton X-100 or n-octylglucoside dissociate mTOR and mLST8 from a complex of Protor-1, Sin1 and Rictor. We also provide evidence that Rictor regulates the expression of Protor-1, and that Protor-1 is not required for the assembly of other mTORC2 subunits into a complex. Protor-1 is a novel Rictor-binding subunit of mTORC2, but further work is required to establish its role.

A role for the actin cytoskeleton in the hormonal and growth-factor-mediated activation of protein kinase B

2001 ◽  
Vol 353 (3) ◽  
pp. 735
Author(s):  
K. PEYROLLIER ◽  
E. HAJDUCH ◽  
A. GRAY ◽  
G. J. LITHERLAND ◽  
A. R. PRESCOTT ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Kinase B
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