Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

5.0K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
5.0K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

6.0K
The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
6.0K
Regulated mRNA Transport02:22

Regulated mRNA Transport

7.1K
In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
7.1K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

8.9K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
8.9K
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

8.2K
Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
8.2K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

6.8K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
6.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Control of lysosome function by the GTPase-activating protein TBC1D9B and its binding partner TMEM55B.

Nature communications·2026
Same author

Community-developed checklists for publishing images and image analyses.

Nature methods·2023
Same author

Conditional deletion of Nedd4-2 in lung epithelial cells causes progressive pulmonary fibrosis in adult mice.

Nature communications·2020
Same author

Control of Akt activity and substrate phosphorylation in cells.

IUBMB life·2020
Same author

Phosphoinositides in the control of lysosome function and homeostasis.

Biochemical Society transactions·2019
Same author

Getting the Akt Together: Guiding Intracellular Akt Activity by PI3K.

Biomolecules·2019

Related Experiment Video

Updated: Mar 8, 2026

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale
10:56

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale

Published on: May 17, 2014

70.0K

Localization of mTORC2 activity inside cells.

Michael Ebner1,2, Benjamin Sinkovics2,3, Magdalena Szczygieł4

  • 1Max F. Perutz Laboratories, Department of Structural and Computational Biology, Vienna BioCenter, 1030 Vienna, Austria.

The Journal of Cell Biology
|February 2, 2017
PubMed
Summary
This summary is machine-generated.

Growth factors regulate cell growth by influencing mammalian target of rapamycin (mTOR) complex 2 (mTORC2) activity. This study reveals mTORC2

More Related Videos

A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation
09:37

A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation

Published on: March 15, 2018

14.8K
Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
08:04

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method

Published on: October 23, 2018

19.9K

Related Experiment Videos

Last Updated: Mar 8, 2026

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale
10:56

Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale

Published on: May 17, 2014

70.0K
A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation
09:37

A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation

Published on: March 15, 2018

14.8K
Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
08:04

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method

Published on: October 23, 2018

19.9K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mammalian target of rapamycin (mTOR) complex 2 (mTORC2) phosphorylates protein kinase Akt, linking extracellular signals to cell growth and proliferation.
  • The precise mechanisms by which growth factors regulate mTORC2 activity towards Akt remain largely uncharacterized.

Purpose of the Study:

  • To investigate the intracellular localization and regulation of mTORC2 activity by growth factors.
  • To develop a reporter system for monitoring endogenous mTORC2 activity and localization.

Main Methods:

  • Utilized advanced imaging techniques and biochemical assays.
  • Examined the localization of mSin1, an essential component of mTORC2.
  • Developed a novel reporter for intracellular mTORC2 activity.

Main Results:

  • Demonstrated that mTORC2 activity is localized to the plasma membrane, mitochondria, and endosomal vesicles within cells.
  • Showed that plasma membrane-localized mTORC2, via the Sin1 pleckstrin homology domain, is independent of phosphoinositide 3-kinase (PI3K) and growth factors.
  • Confirmed that recruitment to the membrane is sufficient for growth factor-induced Akt phosphorylation.

Conclusions:

  • Identified spatially distinct mTORC2 populations with differential sensitivity to PI3K within cells.
  • Suggests that intracellular localization plays a crucial role in regulating mTORC2 activity towards Akt.