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

cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

9.4K
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,...
9.4K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

19.6K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
19.6K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

9.4K
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...
9.4K
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

7.9K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
7.9K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

8.0K
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...
8.0K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

6.5K
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...
6.5K

You might also read

Related Articles

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

Sort by
Same author

TIR-like NADases act in bacterial immunity and the RNA vault.

bioRxiv : the preprint server for biology·2026
Same author

Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Silencing lipid catabolism determines longevity in response to fasting.

Nature communications·2026
Same author

Bacterial ubiquitin ligase engineered for small molecule and protein target identification.

The EMBO journal·2026
Same author

Inhibition of FicD-mediated AMPylation and deAMPylation by Isoprenoid Diphosphates.

bioRxiv : the preprint server for biology·2025
Same author

Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: Apr 15, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

8.7K

The secretory pathway kinases.

Anju Sreelatha1, Lisa N Kinch2, Vincent S Tagliabracci1

  • 1Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Biochimica Et Biophysica Acta
|April 12, 2015
PubMed
Summary
This summary is machine-generated.

Researchers discovered novel kinases in the secretory pathway that phosphorylate extracellular proteins. These kinases are crucial for cellular events and their mutations cause human diseases, highlighting the importance of extracellular protein phosphorylation.

Keywords:
Fam20CKinasesRaine syndromeSecretory pathway

More Related Videos

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

3.0K
Assaying the Kinase Activity of LRRK2 in vitro
06:09

Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

23.1K

Related Experiment Videos

Last Updated: Apr 15, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

8.7K
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

3.0K
Assaying the Kinase Activity of LRRK2 in vitro
06:09

Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

23.1K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Protein phosphorylation is a vital post-translation modification in cellular processes.
  • The kinases responsible for phosphorylating secreted proteins were previously unknown.
  • Extracellular protein phosphorylation has been observed but poorly understood.

Purpose of the Study:

  • To identify and characterize kinases involved in the phosphorylation of proteins within the secretory pathway.
  • To understand the role of these novel kinases in regulating extracellular processes.
  • To investigate the link between mutations in these kinases and human diseases.

Main Methods:

  • Genome sequencing and genetic studies were employed to discover novel kinases.
  • Localization studies identified kinases within the endoplasmic reticulum, Golgi apparatus, and extracellular space.
  • Functional assays were used to determine the substrates and regulatory roles of these kinases.

Main Results:

  • A new class of kinases localized to the secretory pathway was discovered.
  • These kinases were found to phosphorylate extracellular proteins and proteoglycans.
  • Mutations in these kinases are associated with human diseases, confirming their biological significance.

Conclusions:

  • Novel kinases residing in the secretory pathway play a critical role in extracellular protein phosphorylation.
  • These findings elucidate a previously mysterious aspect of protein modification and have implications for understanding disease.
  • Further research into these kinases may lead to therapeutic strategies for related human diseases.