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

PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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 rapamycin-insensitive companion...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

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...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

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...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

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...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

You might also read

Related Articles

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

Sort by
Same author

Low work ability and high disability burden in Cushing's syndrome: a multicenter cohort study.

Journal of endocrinological investigation·2026
Same author

Three-week actigraphy to assess sleep behaviour and circadian rest-activity patterns in suspected and confirmed Cushing's syndrome: an exploratory prospective cohort study.

Pituitary·2026
Same author

Pharmacological Inhibition of FKBP51 Mitigates Early Life Adversity-Induced Social Deficits in Male Mice.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Phaeochromocytomas and paragangliomas harbour tumour-initiating SOX2+ stem cells.

Endocrine-related cancer·2026
Same author

Correction: Discovery of fully synthetic FKBP12-mTOR molecular glues.

Chemical science·2026
Same author

Risk of recurrence after successful surgery for Cushing's disease and association with USP8 genotype and tumour size: an international, retrospective, longitudinal cohort study.

The lancet. Diabetes & endocrinology·2026

Related Experiment Video

Updated: May 9, 2026

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants
07:38

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

FKBPs and the Akt/mTOR pathway.

Felix Hausch1, Christian Kozany, Marily Theodoropoulou

  • 1Max Planck Institute of Psychiatry; Munich, Germany.

Cell Cycle (Georgetown, Tex.)
|July 11, 2013
PubMed
Summary
This summary is machine-generated.

FK506-binding proteins (FKBP) are key to rapamycin

Keywords:
AktFK506 binding proteinFKBPPKBmTORrapamycin

More Related Videos

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

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway
07:15

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway

Published on: August 23, 2024

Related Experiment Videos

Last Updated: May 9, 2026

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants
07:38

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

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

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway
07:15

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway

Published on: August 23, 2024

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • FK506-binding proteins (FKBP) are immunophilins crucial for FK506 and rapamycin immunosuppression.
  • Rapamycin's immunosuppressive function involves FKBP binding to the kinase mTOR, forming inhibitory complexes.
  • FKBP12 was considered essential for rapamycin's gain-of-function, but larger FKBPs can also substitute.

Purpose of the Study:

  • To explore the role of FK506-binding proteins in rapamycin's mechanism of action.
  • To investigate the intrinsic effects of FK506-binding proteins on Akt-mTOR signaling independently of rapamycin.

Main Methods:

  • Review of recent studies on FKBP function in mammalian cells.
  • Analysis of FKBP interactions with mTOR and their impact on signaling pathways.
  • Discussion of FKBP's role in both rapamycin-mediated and intrinsic Akt-mTOR modulation.

Main Results:

  • Larger FK506-binding proteins can functionally replace FKBP12 in mammalian cells.
  • FK506-binding proteins modulate Akt-mTOR signaling even without rapamycin.
  • FKBP's role extends beyond rapamycin's mechanism to intrinsic pathway regulation.

Conclusions:

  • The role of FK506-binding proteins in rapamycin's immunosuppressive effects is broader than previously thought.
  • FK506-binding proteins possess intrinsic functions in regulating the Akt/mTOR pathway.
  • Understanding FKBP's multifaceted roles is crucial for both immunosuppression and cancer therapy research.